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1vz2

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(New page: 200px<br /> <applet load="1vz2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vz2, resolution 2.2&Aring;" /> '''PROLYL OLIGOPEPTIDAS...)
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==About this Structure==
==About this Structure==
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1VZ2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZ2 OCA]].
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1VZ2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Structure known Active Site: AS1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZ2 OCA]].
==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15210359 15210359]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15210359 15210359]
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[[Category: Prolyl oligopeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:45:48 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:15:19 2007''

Revision as of 12:10, 30 October 2007


1vz2, resolution 2.2Å

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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T 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 ... [(full description)]

About this Structure

1VZ2 is a [Single protein] structure of sequence from [Sus scrofa] with GOL as [ligand]. Active as [Prolyl oligopeptidase], with EC number [3.4.21.26]. Structure known Active Site: AS1. Full crystallographic information is available from [OCA].

Reference

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 Tue Oct 30 14:15:19 2007

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