| Structural highlights
2wri is a 25 chain structure with sequence from Escherichia coli and Thermus thermophilus. The January 2010 RCSB PDB Molecule of the Month feature on 70S Ribosomes by David Goodsell is 10.2210/rcsb_pdb/mom_2010_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , ,
| | NonStd Res: | |
| Related: | 2wrj, 2wrk, 2wrl, 1ibk, 1ibl, 2uuc, 2wdk, 2j02, 1j5e, 2j00, 1hnx, 2b9o, 2wh3, 2uub, 1vov, 1emi, 1pnx, 2v46, 2efg, 2vqf, 2wh1, 1n32, 1elo, 2f4v, 1twt, 1qzc, 2uxd, 1fka, 1fjg, 1n36, 2uxc, 1hnw, 1l1u, 1hr0, 2v48, 2b64, 1xmq, 1dar, 2b9m, 1pn8, 2wdg, 1xnr, 1hnz, 1dv4, 1rss, 2wdh, 1jgq, 1i94, 1i96, 2uu9, 1pn7, 1eg0, 1ibm, 2uxb, 2vqe, 1g1x, 2uua, 1i95, 1xnq, 1qd7, 1gix, 1efg, 1jgo, 1jgp, 1n34, 1n33, 1pns, 1yl4, 2wdm, 1xmo, 1i97, 2w2n, 2wrr, 2wrq, 2wro, 2wrn |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.
The structure of the ribosome with elongation factor G trapped in the posttranslocational state.,Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V Science. 2009 Oct 30;326(5953):694-9. PMID:19833919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V. The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science. 2009 Oct 30;326(5953):694-9. PMID:19833919
|
