1vzw
From Proteopedia
| Line 22: | Line 22: | ||
[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:20:30 2007'' |
Revision as of 14:15, 30 October 2007
|
CRYSTAL STRUCTURE OF THE BIFUNCTIONAL PROTEIN PRIA
Overview
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 ... [(full description)]
About 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].
Reference
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
Page seeded by OCA on Tue Oct 30 16:20:30 2007
