1ebb: Difference between revisions
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[[Category: broad specificity phosphatase; dpgm homolog]] | [[Category: broad specificity phosphatase; dpgm homolog]] | ||
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Revision as of 13:05, 30 October 2007
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BACILLUS STEAROTHERMOPHILUS YHFR
Overview
The crystal structure of Bacillus stearothermophilus PhoE (originally, termed YhfR), a broad specificity monomeric phosphatase with a molecular, mass of approximately 24 kDa, has been solved at 2.3 A resolution in order, to investigate its structure and function. PhoE, already identified as a, homolog of a cofactor-dependent phosphoglycerate mutase, shares with the, latter an alpha/beta/alpha sandwich structure spanning, as a structural, excursion, a smaller subdomain composed of two alpha-helices and one short, beta-strand. The active site contains residues from both the, alpha/beta/alpha sandwich and the sub-domain. With the exception of the, hydrophilic catalytic machinery conserved throughout the, cofactor-dependent phosphoglycerate mutase family, the active-site cleft, is strikingly ... [(full description)]
About this Structure
1EBB is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with SO4 and GOL as [ligands]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity., Rigden DJ, Mello LV, Setlow P, Jedrzejas MJ, J Mol Biol. 2002 Feb 1;315(5):1129-43. PMID:11827481
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