4V89
Crystal Structure of Release Factor RF3 Trapped in the GTP State on a Rotated Conformation of the Ribosome (without viomycin)
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Summary for 4V89
| Entry DOI | 10.2210/pdb4v89/pdb |
| Related | 3SFS 3SGF |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total) |
| Functional Keywords | typeii release factor binding with ribosome, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 58 |
| Total formula weight | 2264284.69 |
| Authors | Zhou, J.,Lancaster, L.,Trakhanov, S.,Noller, H.F. (deposition date: 2011-11-17, release date: 2014-07-09, Last modification date: 2024-11-06) |
| Primary citation | Zhou, 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: 22187675DOI: 10.1261/rna.031187.111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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