1vz3: Difference between revisions

Revision as of 16:38, 21 February 2008

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT

OverviewOverview

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.

About this StructureAbout this Structure

1VZ3 is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Prolyl oligopeptidase, with EC number 3.4.21.26 Known structural/functional Site: . 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 Thu Feb 21 15:38:48 2008

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OCA

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 ==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.
+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.
 ==About this Structure==
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 [[Category: serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:17:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:48 2008''