2p99
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E. coli methionine aminopeptidase monometalated with inhibitor YE6
OverviewOverview
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 StructureAbout this Structure
2P99 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.
ReferenceReference
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):5735-5742. Epub 2007 Oct 19. PMID:17948983
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