1xtz
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(New page: 200px<br /><applet load="1xtz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xtz, resolution 2.10Å" /> '''Crystal structure of...)
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Revision as of 04:13, 21 November 2007
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Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes
Overview
Ribose-5-phosphate isomerase A has an important role in sugar metabolism, by interconverting ribose-5-phosphate and ribulose-5-phosphate. This, enzyme is ubiquitous and highly conserved among the three kingdoms of, life. We have solved the 2.1 A resolution crystal structure of the, Saccharomyces cerevisiae enzyme by molecular replacement. This protein, adopts the same fold as its archaeal and bacterial orthologs with two, alpha/beta domains tightly packed together. Mapping of conserved residues, at the surface of the protein reveals strong invariability of the active, site pocket, suggesting a common ligand binding mode and a similar, catalytic mechanism. The yeast enzyme associates as a homotetramer, similarly to the archaeal protein. The effect of an inactivating mutation, (Arg189 to Lys) is discussed in view of the information brought by this, structure.
About this Structure
1XTZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ribose-5-phosphate isomerase, with EC number 5.3.1.6 Full crystallographic information is available from OCA.
Reference
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes., Graille M, Meyer P, Leulliot N, Sorel I, Janin J, Van Tilbeurgh H, Quevillon-Cheruel S, Biochimie. 2005 Aug;87(8):763-9. Epub 2005 Apr 5. PMID:16054529
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