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2wrl

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2wrl, resolution 3.60Å ()
Non-Standard Residues:
Related: 2wri, 2wrj, 2wrk, 2wdi, 2v47, 2wh4, 2wh2, 2wdl, 2b9p, 1yl3, 2v49, 1giy, 2b66, 1v8q, 2j03, 2j01, 2wdn, 1gd8, 1wki, 2b9n, 2wdj, 2wrr, 2wrn, 2wrq, 2wro
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

THE STRUCTURE OF THE RIBOSOME WITH ELONGATION FACTOR G TRAPPED IN THE POST-TRANSLOCATIONAL STATE. (PART 4 OF 4).

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2wrl is a 36 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

See Also

Reference

  • 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

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