1dsb: Difference between revisions

Revision as of 23:32, 30 June 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:1dsb.png

Template:STRUCTURE 1dsb

CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVOCRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO

Template:ABSTRACT PUBMED 8413591

About this StructureAbout this Structure

1DSB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the DsbA protein required for disulphide bond formation in vivo., Martin JL, Bardwell JC, Kuriyan J, Nature. 1993 Sep 30;365(6445):464-8. PMID:8413591

Page seeded by OCA on Mon Jun 30 23:32:35 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1dsb.gif|left|200px]]
+{{Seed}}
+[[Image:1dsb.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dsb|  PDB=1dsb  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO'''
+===CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO===
-==Overview==
+<!--
-Proteins that contain disulphide bonds are often slow to fold in vitro because the oxidation and correct pairing of the cysteine residues is rate limiting. The folding of such proteins is greatly accelerated in Escherichia coli by DsbA, but the mechanism of this rate enhancement is not well understood. Here we report the crystal structure of oxidized DsbA and show that it resembles closely the ubiquitous redox protein thioredoxin, despite very low sequence similarity. An important difference, however, is the presence of another domain which forms a cap over the thioredoxin-like active site of DsbA. The redox-active disulphide bond, which is responsible for the oxidation of substrates, is thus at a domain interface and is surrounded by grooves and exposed hydrophobic side chains. These features suggest that DsbA might act by binding to partially folded polypeptide chains before oxidation of cysteine residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_8413591}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8413591 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8413591}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Martin, J L.]]
 [[Category: Disulfide oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:12:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:32:35 2008''