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| - | [[Image:1wlr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1wlr| PDB=1wlr | SCENE= }} | | {{STRUCTURE_1wlr| PDB=1wlr | SCENE= }} |
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| - | '''Apo aminopeptidase P from E. coli'''
| + | ===Apo aminopeptidase P from E. coli=== |
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| - | ==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}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pita-bread fold]] | | [[Category: Pita-bread fold]] |
| | [[Category: Proline-specific peptidase]] | | [[Category: Proline-specific peptidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:51:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:04:46 2008'' |
Revision as of 13:04, 29 July 2008
Template:STRUCTURE 1wlr
Apo aminopeptidase P from E. coli
Template:ABSTRACT PUBMED 16229471
About this Structure
1WLR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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