2p98

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{{STRUCTURE_2p98| PDB=2p98 | SCENE= }}
{{STRUCTURE_2p98| PDB=2p98 | SCENE= }}
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'''E. coli methionine aminopeptidase monometalated with inhibitor YE7'''
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===E. coli methionine aminopeptidase monometalated with inhibitor YE7===
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==Overview==
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Two divalent metal ions are commonly seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal ions is directly involved in catalysis. Although ample structural and functional information is available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometalated enzyme under physiological conditions. Information on structure, as well as catalysis and inhibition, of the monometalated enzyme is lacking. By improving conditions of high-throughput screening, we identified a unique inhibitor with specificity toward the monometalated enzyme. Kinetic characterization indicates a mutual exclusivity in binding between the inhibitor and the second metal ion at the active site. This is confirmed by X-ray structure, and this inhibitor coordinates with the first metal ion and occupies the space normally occupied by the second metal ion. Kinetic and structural analyses of the inhibition by this and other inhibitors provide insight in designing effective inhibitors of methionine aminopeptidase.
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==About this Structure==
==About this Structure==
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[[Category: Monometalated]]
[[Category: Monometalated]]
[[Category: Mononuclear]]
[[Category: Mononuclear]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:59:58 2008''

Revision as of 14:00, 28 July 2008

Image:2p98.png

Template:STRUCTURE 2p98

E. coli methionine aminopeptidase monometalated with inhibitor YE7

Template:ABSTRACT PUBMED 17948983

About this Structure

2P98 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis., Huang M, Xie SX, Ma ZQ, Huang QQ, Nan FJ, Ye QZ, J Med Chem. 2007 Nov 15;50(23):5735-42. Epub 2007 Oct 19. PMID:17948983

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