1dsb: Difference between revisions

Revision as of 13:19, 21 February 2008

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

OverviewOverview

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.

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 Thu Feb 21 12:19:54 2008

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OCA

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-[[Image:1dsb.gif|left|200px]]<br /><applet load="1dsb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dsb.gif|left|200px]]<br /><applet load="1dsb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dsb, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO'''<br />
 ==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.
+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.
 ==About this Structure==
-DSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DSB OCA].
+DSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSB OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bardwell, J.C.A.]]
+[[Category: Bardwell, J C.A.]]
 [[Category: Kuriyan, J.]]
-[[Category: Martin, J.L.]]
+[[Category: Martin, J L.]]
 [[Category: disulfide oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:32:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:54 2008''