1fon: Difference between revisions

Revision as of 03:41, 1 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:1fon.png

Template:STRUCTURE 1fon

CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN ECRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E

Template:ABSTRACT PUBMED 8168476

About this StructureAbout this Structure

1FON is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E., Pignol D, Gaboriaud C, Michon T, Kerfelec B, Chapus C, Fontecilla-Camps JC, EMBO J. 1994 Apr 15;13(8):1763-71. PMID:8168476

Page seeded by OCA on Tue Jul 1 03:41:38 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fon.gif|left|200px]]
+{{Seed}}
+[[Image:1fon.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fon|  PDB=1fon  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E'''
+===CRYSTAL STRUCTURE OF BOVINE PROCARBOXYPEPTIDASE A-S6 SUBUNIT III, A HIGHLY STRUCTURED TRUNCATED ZYMOGEN E===
-==Overview==
+<!--
-Subunit III, a defective serine endopeptidase lacking the typical N-terminal hydrophobic dipeptide is secreted by the pancreas of ruminant species as part of the bovine ternary complex procarboxypeptidase A-S6. Two monoclinic crystal forms were obtained and subsequently used to solve its X-ray structure. The highest resolution model of subunit III was refined at 1.7 A resolution to a crystallographic R-factor of 18.4%, with r.m.s. bond deviations from ideality of 0.012 A. About 80% of the model presents the characteristic architecture of trypsin-like proteases. The remaining zones, however, have well-defined, unique conformations. The regions from residues 70 to 80 and from 140 to 155 present maximum distances of 16 and 18 A relative to serine proteases and zymogens. Comparisons with the structures of porcine elastase 1 and chymotrypsinogen A indicate that the specific binding pocket of subunit III adopts a zymogen-like conformation and thus provide a basis for its inactivity. In general, the structural analysis of subunit III strongly suggests that it corresponds to a truncated version of a new class of highly structured elastase-like zymogen molecules. Based on the structures of subunit III and elastase 1, it is concluded that large concerted movements are necessary for the activation of zymogen E.
+The line below this paragraph, {{ABSTRACT_PUBMED_8168476}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8168476 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8168476}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Serine protease]]
 [[Category: Truncated zymogen e]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:34:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:41:38 2008''