2v9v: Difference between revisions

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.

2V9V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with CL and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V9V OCA].  

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