This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bhb
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2bhb. | + | [[Image:2bhb.jpg|left|200px]]<br /><applet load="2bhb" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bhb" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2bhb, resolution 2.41Å" /> | caption="2bhb, resolution 2.41Å" /> | ||
'''ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P'''<br /> | '''ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BHB 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 MRD 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] | + | 2BHB 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 MRD 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:Mrd Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHB OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 27: | ||
[[Category: proline-specific peptidase]] | [[Category: proline-specific peptidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:46:57 2007'' |
Revision as of 16:37, 18 December 2007
|
ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P
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
2BHB is a Single protein structure of sequence from Escherichia coli with ZN, FLC, MG and MRD 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
Page seeded by OCA on Tue Dec 18 18:46:57 2007
