1vzw
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CRYSTAL STRUCTURE OF THE BIFUNCTIONAL PROTEIN PRIA
OverviewOverview
Some bacterial genomes contain an incomplete set of genes encoding, phosphoribosyl isomerases, raising the question of whether there exists, broadened substrate specificity for the missing gene products. To, investigate the underlying molecular principles of this hypothesis, we, have determined the crystal structure of the bifunctional enzyme PriA from, Streptomyces coelicolor at 1.8 A resolution. It consists of a, (betaalpha)(8)-barrel fold that is assembled by two symmetric, (betaalpha)(4) half-barrels. The structure shows how its active site may, catalyse the isomerization reactions of two different substrates, and we, provide a plausible model of how the smaller of the two substrates could, be bound in two different orientations. Our findings expand the, half-barrel ancestor concept by demonstrating that symmetry-related, half-barrels could provide a smart solution to cope with dual substrate, specificity. The data may help to unravel molecular rationales regarding, how organisms with miniature genomes can keep central biological pathways, functional.
About this StructureAbout this Structure
1VZW is a Single protein structure of sequence from Streptomyces coelicolor with SO4 and GOL as ligands. Structure known Active Site: CAT. Full crystallographic information is available from OCA.
ReferenceReference
Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity., Kuper J, Doenges C, Wilmanns M, EMBO Rep. 2005 Feb;6(2):134-9. PMID:15654319
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