1e5t: Difference between revisions
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'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT''' | {{Structure | ||
|PDB= 1e5t |SIZE=350|CAPTION= <scene name='initialview01'>1e5t</scene>, resolution 1.7Å | |||
|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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E5T is a [ | 1E5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11256612 11256612] | ||
[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: prolyl oligopeptidase]] | [[Category: prolyl oligopeptidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:10 2008'' | ||
Revision as of 08:50, 20 March 2008
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| 1e5t, resolution 1.7Å | |||||||||||||
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| Sites: | AS and SS | ||||||||||||
| Ligands: | GOL | ||||||||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT
Overview
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 Structure
1E5T is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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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