1zs9
From Proteopedia
(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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| - | [[Image:1zs9.gif|left|200px]]<br /> | + | [[Image:1zs9.gif|left|200px]]<br /><applet load="1zs9" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1zs9, resolution 1.70Å" /> | caption="1zs9, resolution 1.70Å" /> | ||
'''Crystal structure of human enolase-phosphatase E1'''<br /> | '''Crystal structure of human enolase-phosphatase E1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous | + | 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== | ||
| - | 1ZS9 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 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1ZS9 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> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1WDH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structure human enolase-phosphatase e1]] | [[Category: structure human enolase-phosphatase e1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:35 2008'' |
Revision as of 14:18, 21 February 2008
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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 as ligand. This structure supersedes 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
Page seeded by OCA on Thu Feb 21 16:18:35 2008
