3VQT
Crystal structure analysis of the translation factor RF3
Summary for 3VQT
Entry DOI | 10.2210/pdb3vqt/pdb |
Related | 3VR1 |
Descriptor | Peptide chain release factor 3, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | translation, release factor, gtpase |
Biological source | Desulfovibrio vulgaris |
Cellular location | Cytoplasm : B8DIL5 |
Total number of polymer chains | 4 |
Total formula weight | 247256.12 |
Authors | Kihira, K.,Shomura, Y.,Shibata, N.,Kitamura, M.,Higuchi, Y. (deposition date: 2012-03-30, release date: 2012-09-05, Last modification date: 2023-11-08) |
Primary citation | Kihira, K.,Shimizu, Y.,Shomura, Y.,Shibata, N.,Kitamura, M.,Nakagawa, A.,Ueda, T.,Ochi, K.,Higuchi, Y. Crystal structure analysis of the translation factor RF3 (release factor 3) Febs Lett., 586:3705-3709, 2012 Cited by PubMed Abstract: The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3',5'-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator. PubMed: 22975312DOI: 10.1016/j.febslet.2012.08.029 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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