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4V85

Crystal Structure of Release Factor RF3 Trapped in the GTP State on a Rotated Conformation of the Ribosome.

This is a non-PDB format compatible entry.
Summary for 4V85
Entry DOI10.2210/pdb4v85/pdb
Related PRD IDPRD_000226
Descriptor16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
Functional Keywordstypeii release factor binding with ribosome, ribosome-antibiotic complex, ribosome/antibiotic
Biological sourceEscherichia coli
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Total number of polymer chains59
Total formula weight2274150.43
Authors
Zhou, J.,Lancaster, L.,Trakhanov, S.,Noller, H.F. (deposition date: 2011-06-13, release date: 2014-07-09, Last modification date: 2024-12-25)
Primary citationZhou, J.,Lancaster, L.,Trakhanov, S.,Noller, H.F.
Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome.
Rna, 18:230-240, 2012
Cited by
PubMed Abstract: The class II release factor RF3 is a GTPase related to elongation factor EF-G, which catalyzes release of class I release factors RF1 and RF2 from the ribosome after termination of protein synthesis. The 3.3 Å crystal structure of the RF3·GDPNP·ribosome complex provides a high-resolution description of interactions and structural rearrangements that occur when binding of this translational GTPase induces large-scale rotational movements in the ribosome. RF3 induces a 7° rotation of the body and 14° rotation of the head of the 30S ribosomal subunit, and itself undergoes inter- and intradomain conformational rearrangements. We suggest that ordering of critical elements of switch loop I and the P loop, which help to form the GTPase catalytic site, are caused by interactions between the G domain of RF3 and the sarcin-ricin loop of 23S rRNA. The rotational movements in the ribosome induced by RF3, and its distinctly different binding orientation to the sarcin-ricin loop of 23S rRNA, raise interesting implications for the mechanism of action of EF-G in translocation.
PubMed: 22187675
DOI: 10.1261/rna.031187.111
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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