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1e5t

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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>
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=
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|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.]]
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[[Category: GOL]]
 
[[Category: alpha/ beta-hydrolase]]
[[Category: alpha/ beta-hydrolase]]
[[Category: amnesia]]
[[Category: amnesia]]
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[[Category: prolyl oligopeptidase]]
[[Category: prolyl oligopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:44 2008''

Revision as of 16:55, 30 March 2008


PDB ID 1e5t

Drag the structure with the mouse to rotate
, 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


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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