1vz2: Difference between revisions
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==Overview== | ==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 . | 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== | ==About this Structure== | ||
1VZ2 is a | 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== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 16:15, 5 November 2007
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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T 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
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.
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
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