4V5F

The structure of the ribosome with elongation factor G trapped in the post-translocational state

This is a non-PDB format compatible entry.

Summary for 4V5F

• Entry DOI: 10.2210/pdb4v5f/pdb
• Related: 1DAR 1DV4 1EFG 1EG0 1ELO 1EMI 1FJG 1FKA 1G1X 1GIX 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 2EFG 2F4V 2J00 2J02 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC 2UXD 2V46 2V48 2VQE 2VQF 2W2N 2WDG 2WDH 2WDK 2WDM 2WH1 2WH3 2WRN 2WRO 2WRQ 2WRR
• Descriptor: 16S ribosomal RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (62 entities in total)
• Functional Keywords: ribosome, zinc-finger, rna-binding, translation, rrna-binding, protein biosynthesis, elongation factor, ribosomal protein, trna-binding, translocation, metal-binding, nucleotide-binding, elongation factor g, ribonucleoprotein, protein synthesis
• Biological source: THERMUS THERMOPHILUS; More
• Cellular location: Cytoplasm: Q5SHN5
• Total number of polymer chains: 124
• Total formula weight: 4772299.85

Authors

Gao, Y.-G.,Selmer, M.,Dunham, C.M.,Weixlbaumer, A.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2009-09-01, release date: 2014-07-09, Last modification date: 2024-10-16)

Primary citation

Gao, Y.G.,Selmer, M.,Dunham, C.M.,Weixlbaumer, A.,Kelley, A.C.,Ramakrishnan, V.
The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
Science, 326:694-699, 2009

PubMed Abstract: 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.

PubMed: 19833919
DOI: 10.1126/science.1179709

Experimental method

X-RAY DIFFRACTION (3.6 Å)