1e5t: Difference between revisions
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|SITE= <scene name='pdbsite=AS:Active+Site,+Catalytic+Triad'>AS</scene> and <scene name='pdbsite=SS:Disulfide+Engineered+Between+Cys78+And+Gln397cys'>SS</scene> | |SITE= <scene name='pdbsite=AS:Active+Site,+Catalytic+Triad'>AS</scene> and <scene name='pdbsite=SS:Disulfide+Engineered+Between+Cys78+And+Gln397cys'>SS</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=1e5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5t OCA], [http://www.ebi.ac.uk/pdbsum/1e5t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e5t RCSB]</span> | |||
}} | }} | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
[[Category: alpha/ beta-hydrolase]] | [[Category: alpha/ beta-hydrolase]] | ||
[[Category: amnesia]] | [[Category: amnesia]] | ||
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[[Category: prolyl oligopeptidase]] | [[Category: prolyl oligopeptidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:44 2008'' | ||
Revision as of 19:55, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| 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, MUTANT
OverviewOverview
Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.
About this StructureAbout this Structure
1E5T is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism., Fulop V, Szeltner Z, Polgar L, EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612
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