1xtz
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Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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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