1vz3: Difference between revisions

Revision as of 18:44, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vz3.png

Template:STRUCTURE 1vz3

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANTPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT

Template:ABSTRACT PUBMED 15210359

About this StructureAbout this Structure

1VZ3 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding., Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L, J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:15210359

Page seeded by OCA on Mon Jul 28 18:44:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT'''
+===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT===
-==Overview==
+<!--
-Prolyl oligopeptidase contains a peptidase domain and its catalytic triad is covered by the central tunnel of a seven-bladed beta-propeller. This domain makes the enzyme an oligopeptidase by excluding large structured peptides from the active site. The apparently rigid crystal structure does not explain how the substrate can approach the catalytic groups. Two possibilities of substrate access were investigated: either blades 1 and 7 of the propeller domain move apart, or the peptidase and/or propeller domains move to create an entry site at the domain interface. Engineering disulfide bridges to the expected oscillating structures prevented such movements, which destroyed the catalytic activity and precluded substrate binding. This indicated that concerted movements of the propeller and the peptidase domains are essential for the enzyme action.
+The line below this paragraph, {{ABSTRACT_PUBMED_15210359}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15210359 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15210359}}
 ==About this Structure==
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 [[Category: Prolyl oligopeptidase]]
 [[Category: Serine protease]]
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