2v9v: Difference between revisions
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==Overview== | ==Overview== | ||
The crystal structure of the first two winged-helix motifs of translation | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ganichkin, O.]] | [[Category: Ganichkin, O.]] | ||
[[Category: Wahl, M | [[Category: Wahl, M C.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: NA]] | [[Category: NA]] | ||
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[[Category: winged-helix domain]] | [[Category: winged-helix domain]] | ||
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Revision as of 16:54, 21 February 2008
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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 CL and NA as ligands. Known structural/functional Site: AC1. 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
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