1vz2: Difference between revisions
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|SITE= <scene name='pdbsite=AS1:Engineered+Disulphide+Bridge'>AS1</scene> | |SITE= <scene name='pdbsite=AS1:Engineered+Disulphide+Bridge'>AS1</scene> | ||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vz2 OCA], [http://www.ebi.ac.uk/pdbsum/1vz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vz2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
[[Category: Rea, D.]] | [[Category: Rea, D.]] | ||
[[Category: alpha/ beta-hydrolase]] | [[Category: alpha/ beta-hydrolase]] | ||
[[Category: amnesia]] | [[Category: amnesia]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:28:57 2008'' | ||
Revision as of 00:28, 31 March 2008
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| , resolution 2.2Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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