2p98
From Proteopedia
(New page: 200px<br /><applet load="2p98" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p98, resolution 1.700Å" /> '''E. coli methionine ...) |
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==Overview== | ==Overview== | ||
| - | Two divalent metal ions are commonly seen in the active-site cavity of | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Inhibition of | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17948983 17948983] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
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[[Category: mononuclear]] | [[Category: mononuclear]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:12 2008'' |
Revision as of 16:27, 21 February 2008
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E. coli methionine aminopeptidase monometalated with inhibitor YE7
Overview
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.
About this Structure
2P98 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Methionyl aminopeptidase, with EC number 3.4.11.18 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
Page seeded by OCA on Thu Feb 21 18:27:12 2008
