2bh3
From Proteopedia
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| - | [[Image:2bh3.jpg|left|200px]]<br /><applet load="2bh3" size=" | + | [[Image:2bh3.jpg|left|200px]]<br /><applet load="2bh3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bh3, resolution 2.40Å" /> | caption="2bh3, resolution 2.40Å" /> | ||
'''ZN SUBSTITUTED E.COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT'''<br /> | '''ZN SUBSTITUTED E.COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, FLC, MG and PRO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=AC1:LEU Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=FLC:'>FLC</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PRO:'>PRO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=AC1:LEU+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proline-specific peptidase]] | [[Category: proline-specific peptidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:23:58 2008'' |
Revision as of 08:23, 3 February 2008
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ZN SUBSTITUTED E.COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT
Overview
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.
About this Structure
2BH3 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Known structural/functional Site: . 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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