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4V9J

70S ribosome translocation intermediate GDPNP-II containing elongation factor EFG/GDPNP, mRNA, and tRNA bound in the pe*/E state.

This is a non-PDB format compatible entry.
Summary for 4V9J
Entry DOI10.2210/pdb4v9j/pdb
Related PRD IDPRD_000226
Descriptor30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (62 entities in total)
Functional Keywordsgdpnp, chimeric hybrid state ribosome, translocation intermediate, ef-g, mrna, trna, ribosome-antibiotic complex, ribosome/antibiotic
Biological sourceThermus thermophilus
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Cellular locationCytoplasm : Q72I01
Total number of polymer chains122
Total formula weight4566590.96
Authors
Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F. (deposition date: 2013-04-23, release date: 2014-07-09, Last modification date: 2023-12-06)
Primary citationZhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F.
Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation.
Science, 340:1236086-1236086, 2013
Cited by
PubMed Abstract: Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with β,γ-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as "pawls" of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation.
PubMed: 23812722
DOI: 10.1126/science.1236086
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.86 Å)
Structure validation

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数据于2024-11-06公开中

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