1zs9
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(New page: 200px<br /> <applet load="1zs9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zs9, resolution 1.70Å" /> '''Crystal structure o...)
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Revision as of 18:33, 12 November 2007
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Crystal structure of human enolase-phosphatase E1
Overview
Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous, methionine salvage pathway that catalyzes the continuous reactions of, 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone, metabolite using Mg2+ as cofactor. In this study, we have determined the, crystal structure of MASA and its complex with a substrate analog to 1.7A, resolution by multi-wavelength anomalous diffraction and molecular, replacement techniques, respectively. The structures support the proposed, mechanism of phosphatase activity and further suggest the probable, mechanism of enolization. We establish a model for substrate binding to, describe in detail the enzymatic reaction and the formation of the, transition state, which will provide insight into the reaction mechanisms, of other enzymes in the same family.
About this Structure
1ZS9 is a Single protein structure of sequence from Homo sapiens with MG as ligand. This structure superseeds the now removed PDB entry 1WDH. Full crystallographic information is available from OCA.
Reference
Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity., Wang H, Pang H, Bartlam M, Rao Z, J Mol Biol. 2005 May 13;348(4):917-26. PMID:15843022
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