2f51
From Proteopedia
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Structure of Trichomonas vaginalis thioredoxin
Overview
The structure of thioredoxin from the anaerobic organism Trichomonas, vaginalis (TvTrx) has been determined at 1.9 angstroms resolution. The, structure is that of a typical thioredoxin: a five-stranded beta-sheet, structure with two alpha-helices on either side. The active site of the, protein carries a Trp-Cys-Gly-Pro-Cys motif, residues 34-38, at the, N-terminus of an alpha-helix (alpha2). The cysteine residues in this motif, form a redox-active disulfide necessary for thioredoxin activity. With, high-resolution data available, it was possible to model numerous, amino-acid side chains in alternate conformations and this includes the, redox-active disulfide cysteine residues. The sample was initially in the, oxidized state and the use of X-rays from an intense third-generation, synchrotron source resulted in partial photoreduction of this labile redox, centre. Comparisons with previously determined thioredoxin structures, indicate that TvTrx is most similar to the human homologue, although the, insertion of three residues between strands beta4 and beta5 makes the, corresponding turn longer and more flexible in TvTrx. In addition, three, significant amino-acid differences are identified on the protein surfaces, near to the active-site Cys35. These residues may contribute to the, interactions that specific thioredoxins form with their cognate, physiological partners.
About this Structure
2F51 is a Single protein structure of sequence from Trichomonas vaginalis. Full crystallographic information is available from OCA.
Reference
High-resolution structure of recombinant Trichomonas vaginalis thioredoxin., Iulek J, Alphey MS, Westrop GD, Coombs GH, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):216-20. Epub 2006, Jan 18. PMID:16421453
Page seeded by OCA on Tue Jan 29 19:27:45 2008
