2v9v
From Proteopedia
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CRYSTAL STRUCTURE OF MOORELLA THERMOACETICA SELB(377-511)
Overview
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.
About this Structure
2V9V is a Single protein structure of sequence from Moorella thermoacetica with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB., Ganichkin O, Wahl MC, Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1075-81. Epub 2007, Sep 19. PMID:17881825
Page seeded by OCA on Wed Jan 23 13:08:48 2008
Categories: Moorella thermoacetica | Single protein | Ganichkin, O. | Wahl, M.C. | CL | NA | Cytoplasm | Gtp-binding | Nucleotide-binding | Protein biosynthesis | Protein conformational change | Protein dynamics | Selenocysteine | Selenoprotein biosynthesis | Transcription elongation factor selb | Winged-helix domain
