1r9g
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(New page: 200px<br /><applet load="1r9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r9g, resolution 2.5Å" /> '''Three-dimensional Str...)
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Revision as of 23:14, 20 November 2007
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Three-dimensional Structure of YaaE from Bacillus subtilis
Overview
The structure of YaaE from Bacillus subtilis was determined at 2.5-A, resolution. YaaE is a member of the triad glutamine aminotransferase, family and functions in a recently identified alternate pathway for the, biosynthesis of vitamin B(6). Proposed active residues include conserved, Cys-79, His-170, and Glu-172. YaaE shows similarity to HisH, a glutaminase, involved in histidine biosynthesis. YaaD associates with YaaE. A homology, model of this protein was constructed. YaaD is predicted to be a, (beta/alpha)(8) barrel on the basis of sequence comparisons. The predicted, active site includes highly conserved residues 211-216 and 233-235., Finally, a homology model of a putative YaaD-YaaE complex was prepared, using the structure of HisH-F as a model. This model predicts that the, ammonia molecule generated by YaaE is channeled through the center of the, YaaD barrel to the putative YaaD active site.
About this Structure
1R9G is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis., Bauer JA, Bennett EM, Begley TP, Ealick SE, J Biol Chem. 2004 Jan 23;279(4):2704-11. Epub 2003 Oct 28. PMID:14585832
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