1wl6: Difference between revisions

Revision as of 09:45, 28 July 2008

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File:1wl6.png

Template:STRUCTURE 1wl6

Mg-substituted form of E. coli aminopeptidase PMg-substituted form of E. coli aminopeptidase P

Template:ABSTRACT PUBMED 16229471

About this StructureAbout this Structure

1WL6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center., Graham SC, Bond CS, Freeman HC, Guss JM, Biochemistry. 2005 Oct 25;44(42):13820-36. PMID:16229471

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-'''Mg-substituted form of E. coli aminopeptidase P'''
+===Mg-substituted form of E. coli aminopeptidase P===
-==Overview==
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-The effect of metal substitution on the activity and structure of the aminopeptidase P (APPro) from Escherichia coli has been investigated. Measurements of activity in the presence of Mn2+, Mg2+, Zn2+, Na+, and Ca2+ show that significant activity is seen only in the Mn-bound form of the enzyme. The addition of Zn2+ to [MnMn(APPro)] is strongly inhibitory. Crystal structures of [MnMn(APPro)], [MgMg(APPro)], [ZnZn(APPro)], [ZnMg(APPro)], [Ca_(APPro)], [Na_(APPro)], and [apo(APPro)] were determined. The structures of [Ca_(APPro)] and [Na_(APPro)] have a single metal atom at their active site. Surprisingly, when a tripeptide substrate (ValProLeu) was soaked into [Na_(APPro)] crystals in the presence of 200 mM Mg2+, the structure had substrate, but no metal, bound at the active site. The structure of apo APPro complexed with ValProLeu shows that the N-terminal amino group of a substrate can be bound at the active site by carboxylate side chains that normally bind the second metal atom, providing a model for substrate binding in a single-metal active enzyme. Structures of [MnMn(APPro)] and [ZnZn(APPro)] complexes of ProLeu, a product inhibitor, in the presence of excess Zn reveal a third metal-binding site, formed by two conserved His residues and the dipeptide inhibitor. A Zn atom bound at such a site would stabilize product binding and enhance inhibition.
+The line below this paragraph, {{ABSTRACT_PUBMED_16229471}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16229471 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16229471}}
 ==About this Structure==
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 [[Category: Pita-bread fold]]
 [[Category: Proline-specific peptidase]]
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