4V5S
The crystal structure of EF-Tu and G24A-tRNA-Trp bound to a cognate codon on the 70S ribosome.
This is a non-PDB format compatible entry.
Summary for 4V5S
| Entry DOI | 10.2210/pdb4v5s/pdb |
| Related | 1DV4 1EG0 1EMI 1FJG 1FKA 1G1X 1GIX 1HA3 1HNW 1HNX 1HNZ 1HR0 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PN7 1PN8 1PNS 1PNX 1QD7 1QZC 1RSS 1TWT 1VOV 1XMO 1XMQ 1XNQ 1XNR 1YL4 2B64 2B9M 2B9O 2C78 2F4V 2J00 2J02 2JL5 2JL7 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC 2UXD 2V46 2V48 2VQE 2VQF 2WDG 2WDH 2WDK 2WDM 2WH1 2WH3 2WRN 2WRQ 2X9R 2X9T 2XFZ 2XG1 2XQD 2XSY 2XUY 2Y0U 2Y0W 2Y0Y 2Y12 |
| Descriptor | 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (61 entities in total) |
| Functional Keywords | ribosome, ef-tu, trna, gdp, kirromycin, g24a, hirsh trna |
| Biological source | THERMUS THERMOPHILUS More |
| Total number of polymer chains | 118 |
| Total formula weight | 4666486.49 |
| Authors | Schmeing, T.M.,Voorhees, R.M.,Ramakrishnan, V. (deposition date: 2010-12-07, release date: 2014-07-09, Last modification date: 2024-11-06) |
| Primary citation | Schmeing, T.M.,Voorhees, R.M.,Kelley, A.C.,Ramakrishnan, V. How Mutations in tRNA Distant from the Anticodon Affect the Fidelity of Decoding. Nat.Struct.Mol.Biol., 18:432-, 2011 Cited by PubMed Abstract: The ribosome converts genetic information into protein by selecting aminoacyl tRNAs whose anticodons base-pair to an mRNA codon. Mutations in the tRNA body can perturb this process and affect fidelity. The Hirsh suppressor is a well-studied tRNA(Trp) harboring a G24A mutation that allows readthrough of UGA stop codons. Here we present crystal structures of the 70S ribosome complexed with EF-Tu and aminoacyl tRNA (native tRNA(Trp), G24A tRNA(Trp) or the miscoding A9C tRNA(Trp)) bound to cognate UGG or near-cognate UGA codons, determined at 3.2-Å resolution. The A9C and G24A mutations lead to miscoding by facilitating the distortion of tRNA required for decoding. A9C accomplishes this by increasing tRNA flexibility, whereas G24A allows the formation of an additional hydrogen bond that stabilizes the distortion. Our results also suggest that each native tRNA will adopt a unique conformation when delivered to the ribosome that allows accurate decoding. PubMed: 21378964DOI: 10.1038/NSMB.2003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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