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Revision as of 13:21, 30 October 2007
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BACILLUS STEAROTHERMOPHILUS PHOE (PREVIOUSLY KNOWN AS YHFR) IN COMPLEX WITH PHOSPHATE
Overview
Bacillus stearothermophilus phosphatase PhoE is a member of the, cofactor-dependent phosphoglycerate mutase superfamily possessing broad, specificity phosphatase activity. Its previous structural determination in, complex with glycerol revealed probable bases for its efficient hydrolysis, of both large, hydrophobic, and smaller, hydrophilic substrates. Here we, report two further structures of PhoE complexes, to higher resolution of, diffraction, which yield a better and thorough understanding of its, catalytic mechanism. The environment of the phosphate ion in the catalytic, site of the first complex strongly suggests an acid-base catalytic, function for Glu83. It also reveals how the C-terminal tail ordering is, linked to enzyme activation on phosphate binding by a different mechanism, ... [(full description)]
About this Structure
1H2E is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with PO4 and EDO as [ligands]. Structure known Active Site: PO4. Full crystallographic information is available from [OCA].
Reference
Structures of phosphate and trivanadate complexes of Bacillus stearothermophilus phosphatase PhoE: structural and functional analysis in the cofactor-dependent phosphoglycerate mutase superfamily., Rigden DJ, Littlejohn JE, Henderson K, Jedrzejas MJ, J Mol Biol. 2003 Jan 17;325(3):411-20. PMID:12498792
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