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3VQT

Crystal structure analysis of the translation factor RF3

Summary for 3VQT
Entry DOI10.2210/pdb3vqt/pdb
Related3VR1
DescriptorPeptide chain release factor 3, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordstranslation, release factor, gtpase
Biological sourceDesulfovibrio vulgaris
Cellular locationCytoplasm : B8DIL5
Total number of polymer chains4
Total formula weight247256.12
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 citationKihira, 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: 22975312
DOI: 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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数据于2025-07-23公开中

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