1e8m
From Proteopedia
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|PDB= 1e8m |SIZE=350|CAPTION= <scene name='initialview01'>1e8m</scene>, resolution 1.5Å | |PDB= 1e8m |SIZE=350|CAPTION= <scene name='initialview01'>1e8m</scene>, resolution 1.5Å | ||
|SITE= <scene name='pdbsite=AS:Active+Site+Catalytic+Triad,+Inhibitor+A+S554a'>AS</scene> | |SITE= <scene name='pdbsite=AS:Active+Site+Catalytic+Triad,+Inhibitor+A+S554a'>AS</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHQ:FORMIC+ACID+BENZYL+ESTER'>PHQ</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=1e8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8m OCA], [http://www.ebi.ac.uk/pdbsum/1e8m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e8m RCSB]</span> | ||
}} | }} | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: PHQ]] | ||
[[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 19:57:30 2008'' |
Revision as of 16:57, 30 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| 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, MUTANT, COMPLEXED WITH INHIBITOR
Overview
Structure determination of the inactive S554A variant of prolyl oligopeptidase complexed with an octapeptide has shown that substrate binding is restricted to the P4-P2' region. In addition, it has revealed a hydrogen bond network of potential catalytic importance not detected in other serine peptidases. This involves a unique intramolecular hydrogen bond between the P1' amide and P2 carbonyl groups and another between the P2' amide and Nepsilon2 of the catalytic histidine 680 residue. It is argued that both hydrogen bonds promote proton transfer from the imidazolium ion to the leaving group. Another complex formed with the product-like inhibitor benzyloxycarbonyl-glycyl-proline, indicating that the carboxyl group of the inhibitor forms a hydrogen bond with the Nepsilon2 of His(680). Because a protonated histidine makes a stronger interaction with the carboxyl group, it offers a possibility of the determination of the real pK(a) of the catalytic histidine residue. This was found to be 6.25, lower than that of the well studied serine proteases. The new titration method gave a single pK(a) for prolyl oligopeptidase, whose reaction exhibited a complex pH dependence for k(cat)/K(m), and indicated that the observed pK(a) values are apparent. The procedure presented may be applicable for other serine peptidases.
About this Structure
1E8M is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue., Fulop V, Szeltner Z, Renner V, Polgar L, J Biol Chem. 2001 Jan 12;276(2):1262-6. PMID:11031266
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