2bhd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bhd.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2bhd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bhd| PDB=2bhd | SCENE= }}
{{STRUCTURE_2bhd| PDB=2bhd | SCENE= }}
-
'''MG SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT'''
+
===MG 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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_16229471}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Product complex]]
[[Category: Product complex]]
[[Category: Proline-specific peptidase]]
[[Category: Proline-specific peptidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:17:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:15:13 2008''

Revision as of 19:15, 27 July 2008

Image:2bhd.png

Template:STRUCTURE 2bhd

MG SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT

Template:ABSTRACT PUBMED 16229471

About this Structure

2BHD is a Protein complex structure of sequences 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

Page seeded by OCA on Sun Jul 27 22:15:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bhd"
Personal tools