1yns

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(New page: 200px<br /> <applet load="1yns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yns, resolution 1.7&Aring;" /> '''Crystal Structure Of...)
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'''Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog'''<br />
'''Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and HPO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YNS OCA].
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1YNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=HPO:'>HPO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNS OCA].
==Reference==
==Reference==
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[[Category: hydrolase fold]]
[[Category: hydrolase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:21:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:14 2008''

Revision as of 14:07, 21 February 2008

Image:1yns.gif

1yns, resolution 1.7Å

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Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

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

1YNS is a Single protein structure of sequence from Homo sapiens with and as ligands. 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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