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.


2bn7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bn7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2bn7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bn7| PDB=2bn7 | SCENE= }}
{{STRUCTURE_2bn7| PDB=2bn7 | SCENE= }}
-
'''MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND ZN'''
+
===MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND ZN===
-
==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 32: Line 36:
[[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 20:31:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:59:36 2008''

Revision as of 21:59, 28 July 2008

Image:2bn7.png

Template:STRUCTURE 2bn7

MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND ZN

Template:ABSTRACT PUBMED 16229471

About this Structure

2BN7 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

Page seeded by OCA on Tue Jul 29 00:59:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bn7"
Personal tools