2V9V
Crystal Structure of Moorella thermoacetica SelB(377-511)
Summary for 2V9V
| Entry DOI | 10.2210/pdb2v9v/pdb |
| Related | 1LVA 1WSU |
| Descriptor | SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | transcription, protein conformational change, transcription elongation factor selb, selenoprotein biosynthesis, protein dynamics, nucleotide-binding, cytoplasm, gtp-binding, selenocysteine, winged-helix domain, protein biosynthesis |
| Biological source | MOORELLA THERMOACETICA |
| Total number of polymer chains | 1 |
| Total formula weight | 15711.29 |
| Authors | Ganichkin, O.,Wahl, M.C. (deposition date: 2007-08-27, release date: 2007-09-11, Last modification date: 2023-12-13) |
| Primary citation | Ganichkin, O.,Wahl, M.C. Conformational Switches in Winged-Helix Domains 1 and 2 of Bacterial Translation Elongation Factor Selb. Acta Crystallogr.,Sect.D, 63:1075-, 2007 Cited by PubMed Abstract: The crystal structure of the first two winged-helix motifs of translation elongation factor SelB from Moorella thermoacetica has been determined at 1.1 A resolution. Compared with the previous structure of the two domains in conjunction with winged-helix modules 3 and 4, the first winged-helix domain underwent a substantial conformational change during which the alpha-helical and beta-sheet portions of the element opened up like a shell. This conformational rearrangement was elicited by a change in the orientation of Trp396, leading to the disclosure of a bona fide ligand-binding site in the direct vicinity of Trp396. Additionally, the C-terminal tail of the second domain followed a different path compared with the previous structure. It is conceivable that these conformational switches constitute part of the molecular mechanism that underlies the communication between the N-terminal part of SelB, which binds Sec-tRNA(Sec) and GTP, and the C-terminal part of the protein, which binds selenocysteine-insertion sequences. PubMed: 17881825DOI: 10.1107/S0907444907042229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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