1e8n: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1e8n.jpg|left|200px]]<br /><applet load="1e8n" size=" | [[Image:1e8n.jpg|left|200px]]<br /><applet load="1e8n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1e8n, resolution 1.5Å" /> | caption="1e8n, resolution 1.5Å" /> | ||
'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH PEPTIDE'''<br /> | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH PEPTIDE'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
1E8N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with BE2 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AS:Active Site Catalytic Triad, Peptide At S554a'>AS</scene>. Full crystallographic information is available from [http:// | 1E8N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=BE2:'>BE2</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AS:Active+Site+Catalytic+Triad,+Peptide+At+S554a'>AS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8N OCA]. | ||
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: prolyl oligopeptidase]] | [[Category: prolyl oligopeptidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:38:17 2008'' | ||
Revision as of 10:38, 3 February 2008
|
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH PEPTIDE
OverviewOverview
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 StructureAbout this Structure
1E8N is a Single protein structure of sequence from Sus scrofa with and as ligands. Active as Prolyl oligopeptidase, with EC number 3.4.21.26 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Feb 3 09:38:17 2008