3prk: Difference between revisions

Revision as of 13:03, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3prk.png

Template:STRUCTURE 3prk

INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTIONINHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1894649

About this StructureAbout this Structure

3PRK is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution., Wolf WM, Bajorath J, Muller A, Raghunathan S, Singh TP, Hinrichs W, Saenger W, J Biol Chem. 1991 Sep 15;266(26):17695-9. PMID:1894649

Page seeded by OCA on Thu Jul 3 13:03:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3prk.jpg|left|200px]]
+{{Seed}}
+[[Image:3prk.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3prk|  PDB=3prk  |  SCENE=  }}
-'''INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION'''
+===INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structure of the transition state analog complex formed covalently between proteinase K and methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone was determined by x-ray diffraction methods at a resolution of 2.2 A and refined by constrained least squares to an R factor of 19.8% for the 11864 structure amplitudes greater than 1 sigma F. The chloromethyl ketone group is covalently linked with the active site functional groups His69(N epsilon) and Ser224(O gamma). The former has substituted for chlorine and the latter has attacked the carbon of the ketone group, thereby forming the tetrahedral carbon atom of the transition state analog. The peptide part of the inhibitor is in an extended conformation and fills subsites S1 to S5 of the substrate recognition site. Its backbone hydrogens bond with strands 100-104 and 132-136 of the substrate recognition site as the central strand of a three-stranded antiparallel beta-pleated sheet. This sheet formation is associated with a movement by approximately 1 A of strand 100-104 which is probably associated with the insertion of the bulky proline side chain. The methoxysuccinyl group is stacked on the phenolic side chain of Tyr104 that is a part of the bottom of the recognition site. Biochemical studies show that shorter inhibitors of this type are less effective than the longer one, because there are fewer hydrogen bonding and van der Waals/stacking interactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_1894649}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1894649 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1894649}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Singh, T P.]]
 [[Category: Wolf, W M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:11:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:03:13 2008''