Show notes

Translation

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Chapters

• 0:00 Intro
• 1:12 Finishing the message: splicing
• 2:32 Leaving the nucleus
• 3:19 The ribosome
• 3:38 Loading at the cap, the start codon
• 4:55 Building the chain
• 7:25 Twenty amino acids, one code
• 8:58 Speed, and many ribosomes at once
• 9:20 Stop
• 9:55 An RNA heart
• 11:16 Back to Rubisco

Sources

103 sources. Each was checked against its record (Crossref, PubMed, the Protein Data Bank, or the textbook edition) and against the claim it supports.

Papers

• Agris PF, Vendeix FA & Graham WD (2007). tRNA's wobble decoding of the genome: 40 years of modification. J Mol Biol 366:1-13. doi.org/10.1016/j.jmb.2006.11.046
• Alkalaeva EZ, Pisarev AV, Frolova LY, et al. (2006). In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125:1125-1136. doi.org/10.1016/j.cell.2006.04.035
• Bar-On YM & Milo R (2019). The global mass and average rate of rubisco. Proc Natl Acad Sci U S A 116:4738-4743. doi.org/10.1073/pnas.1816654116
• Bartel DP & Szostak JW (1993). Isolation of new ribozymes from a large pool of random sequences. Science 261:1411-1418. doi.org/10.1126/science.7690155
• Beck M & Hurt E (2017). The nuclear pore complex: understanding its function through structural insight. Nat Rev Mol Cell Biol 18:73-89. doi.org/10.1038/nrm.2016.147
• Bowman JC, Petrov AS, Frenkel-Pinter M, et al. (2020). Root of the Tree: The Significance, Evolution, and Origins of the Ribosome. Chem Rev 120:4848-4878. doi.org/10.1021/acs.chemrev.9b00742
• Brown A, Shao S, Murray J, et al. (2015). Structural basis for stop codon recognition in eukaryotes. Nature 524:493-496. doi.org/10.1038/nature14896
• Brown JW, Smith P & Simpson CG (1996). Arabidopsis consensus intron sequences. Plant Mol Biol 32:531-535. doi.org/10.1007/BF00019105
• Brown SM, Mayer-Bacon C & Freeland S (2023). Xeno Amino Acids: A Look into Biochemistry as We Do Not Know It. Life (Basel) 13:2281. doi.org/10.3390/life13122281
• Cohen Y & Alfonta L (2025). Engineering of the genetic code. Curr Opin Biotechnol 91:103245. doi.org/10.1016/j.copbio.2024.103245
• Ehrnsberger HF, Grasser M & Grasser KD (2019). Nucleocytosolic mRNA transport in plants: export factors and their influence on growth and development. J Exp Bot 70:3757-3763. doi.org/10.1093/jxb/erz173
• Englert M, Moses S, Hohn M, et al. (2013). Aminoacylation of tRNA 2'- or 3'-hydroxyl by phosphoseryl- and pyrrolysyl-tRNA synthetases. FEBS Lett 587:3360-3364. doi.org/10.1016/j.febslet.2013.08.037
• Fox GE (2010). Origin and evolution of the ribosome. Cold Spring Harb Perspect Biol 2:a003483. doi.org/10.1101/cshperspect.a003483
• Hou YM (2010). CCA addition to tRNA: implications for tRNA quality control. IUBMB Life 62:251-260. doi.org/10.1002/iub.301
• Hug LA, Baker BJ, Anantharaman K, et al. (2016). A new view of the tree of life. Nat Microbiol 1:16048. doi.org/10.1038/nmicrobiol.2016.48
• Ingolia NT, Lareau LF & Weissman JS (2011). Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147:789-802. doi.org/10.1016/j.cell.2011.10.002
• Izumi M, Tsunoda H, Suzuki Y, et al. (2012). RBCS1A and RBCS3B, two major members within the Arabidopsis RBCS multigene family, function to yield sufficient Rubisco content for leaf photosynthetic capacity. J Exp Bot 63:2159-2170. doi.org/10.1093/jxb/err434
• Jackson RJ, Hellen CU & Pestova TV (2010). The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11:113-127. doi.org/10.1038/nrm2838
• Jarvis P (2008). Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol 179:257-285. doi.org/10.1111/j.1469-8137.2008.02452.x
• Knight JRP, Garland G, Pöyry T, et al. (2020). Control of translation elongation in health and disease. Dis Model Mech 13:dmm043208. doi.org/10.1242/dmm.043208
• Knockenhauer KE & Schwartz TU (2016). The Nuclear Pore Complex as a Flexible and Dynamic Gate. Cell 164:1162-1171. doi.org/10.1016/j.cell.2016.01.034
• Kondo Y, Oubridge C, van Roon AM & Nagai K (2015). Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein particle, reveals the mechanism of 5' splice site recognition. eLife 4:e04986. doi.org/10.7554/eLife.04986
• Lengyel P (1966). Problems in protein biosynthesis. J Gen Physiol 49:305-330. doi.org/10.1085/jgp.49.6.305
• Liu Z, Luyten I, Bottomley MJ, et al. (2001). Structural basis for recognition of the intron branch site RNA by splicing factor 1. Science 294:1098-1102. doi.org/10.1126/science.1064719
• Mehlin H, Daneholt B & Skoglund U (1992). Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell 69:605-613. doi.org/10.1016/0092-8674(92)90224-z
• Mount SM (1982). A catalogue of splice junction sequences. Nucleic Acids Res 10:459-472. doi.org/10.1093/nar/10.2.459
• Nissen P, Hansen J, Ban N, et al. (2000). The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930. doi.org/10.1126/science.289.5481.920
• Ogle JM, Brodersen DE, Clemons WM Jr, et al. (2001). Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292:897-902. doi.org/10.1126/science.1060612
• Pfaff C, Ehrnsberger HF, Flores-Tornero M, et al. (2018). ALY RNA-Binding Proteins Are Required for Nucleocytosolic mRNA Transport and Modulate Plant Growth and Development. Plant Physiol 177:226-240. doi.org/10.1104/pp.18.00173
• Polacek N & Mankin AS (2005). The ribosomal peptidyl transferase center: structure, function, evolution, inhibition. Crit Rev Biochem Mol Biol 40:285-311. doi.org/10.1080/10409230500326334
• Polikanov YS, Steitz TA & Innis CA (2014). A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome. Nat Struct Mol Biol 21:787-793. doi.org/10.1038/nsmb.2871
• Robertson MP & Joyce GF (2012). The origins of the RNA world. Cold Spring Harb Perspect Biol 4:a003608. doi.org/10.1101/cshperspect.a003608
• Rubio Gomez MA & Ibba M (2020). Aminoacyl-tRNA synthetases. RNA 26:910-936. doi.org/10.1261/rna.071720.119
• Shi H & Moore PB (2000). The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: a classic structure revisited. RNA 6:1091-1105. doi.org/10.1017/s1355838200000364
• Simpson CG, Thow G, Clark GP, et al. (2002). Mutational analysis of a plant branchpoint and polypyrimidine tract required for constitutive splicing of a mini-exon. RNA 8:47-56. doi.org/10.1017/s1355838202015546
• Song H, Mugnier P, Das AK, et al. (2000). The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100:311-321. doi.org/10.1016/s0092-8674(00)80667-4
• Will CL & Lührmann R (2011). Spliceosome structure and function. Cold Spring Harb Perspect Biol 3:a003707. doi.org/10.1101/cshperspect.a003707
• Williams TA, Cox CJ, Foster PG, et al. (2020). Phylogenomics provides robust support for a two-domains tree of life. Nat Ecol Evol 4:138-147. doi.org/10.1038/s41559-019-1040-x
• Wilson RH & Hayer-Hartl M (2018). Complex Chaperone Dependence of Rubisco Biogenesis. Biochemistry 57:3210-3216. doi.org/10.1021/acs.biochem.8b00132
• Wochner A, Attwater J, Coulson A & Holliger P (2011). Ribozyme-catalyzed transcription of an active ribozyme. Science 332:209-212. doi.org/10.1126/science.1200752
• Woese CR, Kandler O & Wheelis ML (1990). Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci U S A 87:4576-4579. doi.org/10.1073/pnas.87.12.4576
• Wu S, Romfo CM, Nilsen TW & Green MR (1999). Functional recognition of the 3' splice site AG by the splicing factor U2AF35. Nature 402:832-835. doi.org/10.1038/45590
• Youngman EM, Brunelle JL, Kochaniak AB & Green R (2004). The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell 117:589-599. doi.org/10.1016/s0092-8674(04)00411-8

Textbooks

• Alberts B, Johnson A, Lewis J, Raff M, Roberts K & Walter P (2002). Molecular Biology of the Cell, 4th ed. New York: Garland Science. Free on NCBI Bookshelf: www.ncbi.nlm.nih.gov/books/NBK21054/ (sections used: From RNA to Protein, www.ncbi.nlm.nih.gov/books/NBK26829/; From DNA to RNA, www.ncbi.nlm.nih.gov/books/NBK26887/)
• Clark MA, Choi J & Douglas M (2018). Biology 2e. OpenStax, Rice University. ISBN 9781947172524. openstax.org/details/books/biology-2e (accessed 2026-10-20)
• Milo R & Phillips R (2015). Cell Biology by the Numbers. Garland Science. ISBN 9781317230694. doi.org/10.1201/9780429258770
• Parker N, Schneegurt M, Tu AHT, Lister P & Forster BM (2016). Microbiology. OpenStax, Rice University. ISBN 9781947172234. openstax.org/details/books/microbiology (accessed 2026-10-20)

Structures drawn

• PDB 9H3G: Structure of the Arabidopsis thaliana 80S ribosome in complex with P- and E-site tRNAs and mRNA. Ko D, Ruonala R, Faille A, et al. (2026). Recruitment of bifunctional regulator thermospermine to methylated ribosomes directs xylem fate. Science 391:694-699. doi.org/10.1126/science.adx2867 doi.org/10.2210/pdb9h3g/pdb
• PDB 6Y0G: Structure of human ribosome in classical-PRE state. Bhaskar V, Graff-Meyer A, Schenk AD, et al. (2020). Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes. Cell Rep 31:107473. doi.org/10.1016/j.celrep.2020.03.037 doi.org/10.2210/pdb6y0g/pdb
• PDB 8G60: mRNA decoding in human is kinetically and structurally distinct from bacteria (CR state). Holm M, Natchiar SK, Rundlet EJ, et al. (2023). mRNA decoding in human is kinetically and structurally distinct from bacteria. Nature 617:200-207. doi.org/10.1038/s41586-023-05908-w doi.org/10.2210/pdb8g60/pdb
• PDB 8CDR: Translocation intermediate 2 (TI-2) of 80S S. cerevisiae ribosome with ligands and eEF2 in the presence of sordarin. Milicevic N, Jenner L, Myasnikov A, et al. (2024). mRNA reading frame maintenance during eukaryotic ribosome translocation. Nature 625:393-400. doi.org/10.1038/s41586-023-06780-4 doi.org/10.2210/pdb8cdr/pdb
• PDB 5LZT: Structure of the mammalian ribosomal termination complex with eRF1 and eRF3. Shao S, Murray J, Brown A, et al. (2016). Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Cell 167:1229-1240.e15. doi.org/10.1016/j.cell.2016.10.046 doi.org/10.2210/pdb5lzt/pdb
• PDB 5LZU: Structure of the mammalian ribosomal termination complex with accommodated eRF1. Shao S, Murray J, Brown A, et al. (2016). Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Cell 167:1229-1240.e15. doi.org/10.1016/j.cell.2016.10.046 doi.org/10.2210/pdb5lzu/pdb
• PDB 8OZ0: Structure of a human 48S translation initiation complex with eIF4F and eIF4A. Brito Querido J, Sokabe M, Diaz-Lopez I, et al. (2024). The structure of a human translation initiation complex reveals two independent roles for the helicase eIF4A. Nat Struct Mol Biol 31:455-464. doi.org/10.1038/s41594-023-01196-0 doi.org/10.2210/pdb8oz0/pdb
• PDB 2IDV: Crystal structure of wheat C113S mutant EIF4E bound TO 7-methyl-GDP. Monzingo AF, Dhaliwal S, Dutt-Chaudhuri A, et al. (2007). The structure of eukaryotic translation initiation factor-4E from wheat reveals a novel disulfide bond. Plant Physiol 143:1504-1518. doi.org/10.1104/pp.106.093146 doi.org/10.2210/pdb2idv/pdb
• PDB 4PJO: Minimal U1 snRNP. Kondo Y, Oubridge C, van Roon AM, Nagai K (2015). Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein particle, reveals the mechanism of 5' splice site recognition. eLife 4:e04986. doi.org/10.7554/eLife.04986 doi.org/10.2210/pdb4pjo/pdb
• PDB 1K1G: Structural basis for recognition of the intron branch site rna by splicing factor 1. Liu Z, Luyten I, Bottomley MJ, et al. (2001). Structural basis for recognition of the intron branch site RNA by splicing factor 1. Science 294:1098-1102. doi.org/10.1126/science.1064719 doi.org/10.2210/pdb1k1g/pdb
• PDB 7C06: Crystal structure of yeast U2AF1 complex bound to 3' splice site RNA, 5'-UAGGU. Yoshida H, Park SY, Sakashita G, et al. (2020). Elucidation of the aberrant 3' splice site selection by cancer-associated mutations on the U2AF1. Nat Commun 11:4744. doi.org/10.1038/s41467-020-18559-6 doi.org/10.2210/pdb7c06/pdb
• PDB 7Q4O: Substrate-bound A-like U2 snRNP. Tholen J, Razew M, Weis F, Galej WP (2022). Structural basis of branch site recognition by the human spliceosome. Science 375:50-57. doi.org/10.1126/science.abm4245 doi.org/10.2210/pdb7q4o/pdb
• PDB 5YZG: The Cryo-EM Structure of Human Catalytic Step I Spliceosome (C complex) at 4.1 angstrom resolution. Zhan X, Yan C, Zhang X, et al. (2018). Structure of a human catalytic step I spliceosome. Science 359:537-545. doi.org/10.1126/science.aar6401 doi.org/10.2210/pdb5yzg/pdb
• PDB 7R5K: Human nuclear pore complex (constricted). Mosalaganti S, Obarska-Kosinska A, Siggel M, et al. (2022). AI-based structure prediction empowers integrative structural analysis of human nuclear pores. Science 376:eabm9506. doi.org/10.1126/science.abm9506 doi.org/10.2210/pdb7r5k/pdb
• PDB 9N37: Cryo-EM structure of Rubisco from Arabidopsis thaliana with the 1A small subunit isoform. Askey B, Ceminsky M, Scott E, et al. (2026). Rubisco kinetic acclimation at the holoenzyme level. Proc Natl Acad Sci USA 123:e2519914123. doi.org/10.1073/pnas.2519914123 doi.org/10.2210/pdb9n37/pdb
• PDB 1QTQ: Glutaminyl-tRNA synthetase complexed with tRNA and an amino acid analog (E. coli; X-ray 2.25 Å; the loading enzyme drawn for line 33, added 2026-10-20, RCSB and PubMed resolved 2026-10-20). Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA (1998). How glutaminyl-tRNA synthetase selects glutamine. Structure 6:439-449. doi.org/10.1016/s0969-2126(98)00046-x doi.org/10.2210/pdb1qtq/pdb
• PDB 5FLM: Structure of transcribing mammalian RNA polymerase II. Bernecky C, Herzog F, Baumeister W, et al. (2016). Structure of Transcribing Mammalian RNA Polymerase II. Nature 529:551-554. doi.org/10.1038/nature16482 doi.org/10.2210/pdb5flm/pdb

Structures in the opening field of proteins

• PDB 4HHB: The crystal structure of human deoxyhaemoglobin at 1.74 angstroms resolution. Fermi G, Perutz MF, Shaanan B, Fourme R (1984). The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. J Mol Biol 175:159-174. doi.org/10.1016/0022-2836(84)90472-8 doi.org/10.2210/pdb4hhb/pdb
• PDB 1GFL: Structure of green fluorescent protein. Yang F, Moss LG, Phillips GN Jr (1996). The molecular structure of green fluorescent protein. Nat Biotechnol 14:1246-1251. doi.org/10.1038/nbt1096-1246 doi.org/10.2210/pdb1gfl/pdb
• PDB 1UBQ: Structure of ubiquitin refined at 1.8 angstroms resolution. Vijay-Kumar S, Bugg CE, Cook WJ (1987). Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194:531-544. doi.org/10.1016/0022-2836(87)90679-6 doi.org/10.2210/pdb1ubq/pdb
• PDB 1LYZ: Real-space refinement of the structure of hen egg-white lysozyme. Diamond R (1974). Real-space refinement of the structure of hen egg-white lysozyme. J Mol Biol 82:371-391. doi.org/10.1016/0022-2836(74)90598-1 doi.org/10.2210/pdb1lyz/pdb
• PDB 1IGT: Structure of immunoglobulin. Harris LJ, Larson SB, Hasel KW, McPherson A (1997). Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 36:1581-1597. doi.org/10.1021/bi962514+ doi.org/10.2210/pdb1igt/pdb
• PDB 1AON: Crystal structure of the asymmetric chaperonin complex groel/groes/(adp)7. Xu Z, Horwich AL, Sigler PB (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-750. doi.org/10.1038/41944 doi.org/10.2210/pdb1aon/pdb
• PDB 1BL8: Potassium channel (kcsa) from streptomyces lividans. Doyle DA, Morais Cabral J, Pfuetzner RA, et al. (1998). The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280:69-77. doi.org/10.1126/science.280.5360.69 doi.org/10.2210/pdb1bl8/pdb
• PDB 1MBN: The stereochemistry of the protein myoglobin. Watson HC (1969). The Stereochemistry of the Protein Myoglobin. Prog Stereochem 4:299. doi.org/10.2210/pdb1mbn/pdb
• PDB 1TIM: Structure of triose phosphate isomerase from chicken muscle. Banner DW, Bloomer A, Petsko GA, et al. (1976). Atomic coordinates for triose phosphate isomerase from chicken muscle. Biochem Biophys Res Commun 72:146-155. doi.org/10.2210/pdb1tim/pdb
• PDB 4INS: The structure of 2zn pig insulin crystals at 1.5 angstroms resolution. Baker EN, Blundell TL, Cutfield JF, et al. (1988). The structure of 2Zn pig insulin crystals at 1.5 A resolution. Philos Trans R Soc Lond B 319:369-456. doi.org/10.2210/pdb4ins/pdb
• PDB 1HSG: Crystal structure at 1.9 angstroms resolution of human immunodeficiency virus (hiv) ii protease complexed with l-735,524, an orally bioavailable inhibitor of the hiv proteases. Chen Z, Li Y, Chen E, et al. (1994). Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases. J Biol Chem 269:26344-26348. doi.org/10.2210/pdb1hsg/pdb
• PDB 1JFF: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol. Lowe J, Li H, Downing KH, Nogales E (2001). Refined structure of alpha beta-tubulin at 3.5 A resolution. J Mol Biol 313:1045-1057. doi.org/10.1006/jmbi.2001.5077 doi.org/10.2210/pdb1jff/pdb
• PDB 1BMF: Bovine mitochondrial f1-atpase. Abrahams JP, Leslie AG, Lutter R, Walker JE (1994). Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370:621-628. doi.org/10.1038/370621a0 doi.org/10.2210/pdb1bmf/pdb
• PDB 1RYP: Crystal structure of the 20s proteasome from yeast at 2.4 angstroms resolution. Groll M, Ditzel L, Lowe J, et al. (1997). Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386:463-471. doi.org/10.1038/386463a0 doi.org/10.2210/pdb1ryp/pdb
• PDB 1STP: Structural origins of high-affinity biotin binding to streptavidin. Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR (1989). Structural origins of high-affinity biotin binding to streptavidin. Science 243:85-88. doi.org/10.2210/pdb1stp/pdb
• PDB 1RWT: Crystal Structure of Spinach Major Light-harvesting complex at 2.72 Angstrom Resolution. Liu Z, Yan H, Wang K, et al. (2004). Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature 428:287-292. doi.org/10.1038/nature02373 doi.org/10.2210/pdb1rwt/pdb
• PDB 1C3W: Bacteriorhodopsin/lipid complex at 1.55 a resolution. Luecke H, Schobert B, Richter HT, et al. (1999). Structure of bacteriorhodopsin at 1.55 A resolution. J Mol Biol 291:899-911. doi.org/10.1006/jmbi.1999.3027 doi.org/10.2210/pdb1c3w/pdb
• PDB 6VXX: Structure of the SARS-CoV-2 spike glycoprotein (closed state). Walls AC, Park YJ, Tortorici MA, et al. (2020). Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell 181:281. doi.org/10.1016/j.cell.2020.02.058 doi.org/10.2210/pdb6vxx/pdb
• PDB 1LCI: Firefly luciferase. Conti E, Franks NP, Brick P (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4:287-298. doi.org/10.1016/s0969-2126(96)00033-0 doi.org/10.2210/pdb1lci/pdb
• PDB 1CLL: Calmodulin structure refined at 1.7 angstroms resolution. Chattopadhyaya R, Meador WE, Means AR, Quiocho FA (1992). Calmodulin structure refined at 1.7 A resolution. J Mol Biol 228:1177-1192. doi.org/10.1016/0022-2836(92)90324-d doi.org/10.2210/pdb1cll/pdb
• PDB 1J4N: Crystal Structure of the AQP1 water channel. Sui H, Han BG, Lee JK, et al. (2001). Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878. doi.org/10.1038/414872a doi.org/10.2210/pdb1j4n/pdb
• PDB 2MYS: Myosin subfragment-1, alpha carbon coordinates only for the two light chains. Rayment I, Rypniewski WR, Schmidt-Base K, et al. (1993). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261:50-58. doi.org/10.2210/pdb2mys/pdb
• PDB 1J6Z: Uncomplexed actin. Otterbein LR, Graceffa P, Dominguez R (2001). The crystal structure of uncomplexed actin in the ADP state. Science 293:708-711. doi.org/10.1126/science.1059700 doi.org/10.2210/pdb1j6z/pdb
• PDB 1MFR: Crystal structure of m ferritin. Ha Y, Shi D, Small W, et al. (1999). Crystal structure of bullfrog M ferritin at 2.8 A resolution: analysis of subunit interactions and the binuclear metal center. J Biol Inorg Chem 4:243-256. doi.org/10.1007/s007750050310 doi.org/10.2210/pdb1mfr/pdb
• PDB 7CAT: The NADPH binding site on beef liver catalase. Fita I, Rossmann MG (1985). The NADPH binding site on beef liver catalase. Proc Natl Acad Sci USA 82:1604-1608. doi.org/10.1073/pnas.82.6.1604 doi.org/10.2210/pdb7cat/pdb
• PDB 4OO8: Crystal structure of Streptococcus pyogenes Cas9 in complex with guide RNA and target DNA. Nishimasu H, Ran FA, Hsu PD, et al. (2014). Crystal structure of Cas9 in complex with guide RNA and target DNA. Cell 156:935-949. doi.org/10.1016/j.cell.2014.02.001 doi.org/10.2210/pdb4oo8/pdb
• PDB 1OCC: Structure of bovine heart cytochrome c oxidase at the fully oxidized state. Tsukihara T, Aoyama H, Yamashita E, et al. (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science 272:1136-1144. doi.org/10.2210/pdb1occ/pdb
• PDB 1EFT: The crystal structure of elongation factor ef-tu from thermus aquaticus in the gtp conformation. Kjeldgaard M, Nissen P, Thirup S, Nyborg J (1993). The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1:35-50. doi.org/10.1016/0969-2126(93)90007-4 doi.org/10.2210/pdb1eft/pdb
• PDB 2C9M: Structure of (SR) Calcium-ATPase in the Ca2E1 state solved in a P1 crystal form. Lund Jensen AM, Sorensen TLM, Olesen C, et al. (2006). Modulatory and Catalytic Modes of ATP Binding by the Calcium Pump. EMBO J 25:2305. doi.org/10.1038/sj.emboj.7601135 doi.org/10.2210/pdb2c9m/pdb
• PDB 1PRC: Crystallographic refinement at 2.3 angstroms resolution and refined model of the photosynthetic reaction center from rhodopseudomonas viridis. Deisenhofer J, Epp O, Sinning I, Michel H (1995). Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol 246:429-457. doi.org/10.1006/jmbi.1994.0097 doi.org/10.2210/pdb1prc/pdb
• PDB 1TAU: Taq polymerase (e.c.2.7.7.7)/dna/b-octylglucoside complex. Eom SH, Wang J, Steitz TA (1996). Structure of Taq ploymerase with DNA at the polymerase active site. Nature 382:278-281. doi.org/10.1038/382278a0 doi.org/10.2210/pdb1tau/pdb
• PDB 2PTC: The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Marquart M, Walter J, Deisenhofer J, et al. (1983). The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors. Acta Crystallogr B 39:480. doi.org/10.2210/pdb2ptc/pdb
• PDB 1CRN: Water structure of a hydrophobic protein at atomic resolution. pentagon rings of water molecules in crystals of crambin. Teeter MM (1984). Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin. Proc Natl Acad Sci USA 81:6014-6018. doi.org/10.1073/pnas.81.19.6014 doi.org/10.2210/pdb1crn/pdb
• PDB 1F88: Crystal structure of bovine rhodopsin. Palczewski K, Kumasaka T, Hori T, et al. (2000). Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739-745. doi.org/10.1126/science.289.5480.739 doi.org/10.2210/pdb1f88/pdb

Sequences and databases

• NCBI RefSeq NM_105379.4. Arabidopsis thaliana ribulose bisphosphate carboxylase small chain 1A (RBCS1A), mRNA. www.ncbi.nlm.nih.gov/nuccore/NM_105379.4
• NCBI GenBank AK319060.1. Arabidopsis thaliana AT1G67090 mRNA, complete cds, clone RAFL25-30-K13 (source of the 5′ end drawn). www.ncbi.nlm.nih.gov/nuccore/AK319060.1
• UniProtKB P10795 (RBS1A_ARATH). Ribulose bisphosphate carboxylase small subunit 1A, chloroplastic; Arabidopsis thaliana; 180 aa; transit peptide 1-54. www.uniprot.org/uniprotkb/P10795
• AlphaFold Protein Structure Database, model AF-Q8L773-F1 (UniProtKB Q8L773, THO4A_ARATH, ALY1, Arabidopsis thaliana). alphafold.ebi.ac.uk/entry/Q8L773
• wwPDB Chemical Component Dictionary (amino-acid side chains). www.wwpdb.org/data/ccd