1qfs: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qfs.gif|left|200px]] | [[Image:1qfs.gif|left|200px]] | ||
'''PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL''' | {{Structure | ||
|PDB= 1qfs |SIZE=350|CAPTION= <scene name='initialview01'>1qfs</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZPR:N-BENZYLOXYCARBONYL-L-PROLYL-L-PROLINAL'>ZPR</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 MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1QFS is a [ | 1QFS 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=1QFS OCA]. | ||
==Reference== | ==Reference== | ||
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis., Fulop V, Bocskei Z, Polgar L, Cell. 1998 Jul 24;94(2):161-70. PMID:[http:// | Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis., Fulop V, Bocskei Z, Polgar L, Cell. 1998 Jul 24;94(2):161-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9695945 9695945] | ||
[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[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 13:36:47 2008'' | ||
Revision as of 14:36, 20 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL
OverviewOverview
Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The 1.4 A resolution crystal structure is presented here. The enzyme contains a peptidase domain with an alpha/beta hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of an unusual beta propeller. This domain makes prolyl oligopeptidase an oligopeptidase by excluding large structured peptides from the active site. In this way, the propeller protects larger peptides and proteins from proteolysis in the cytosol. The structure is also obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders.
About this StructureAbout this Structure
1QFS is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis., Fulop V, Bocskei Z, Polgar L, Cell. 1998 Jul 24;94(2):161-70. PMID:9695945
Page seeded by OCA on Thu Mar 20 13:36:47 2008