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2hi7

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|PDB= 2hi7 |SIZE=350|CAPTION= <scene name='initialview01'>2hi7</scene>, resolution 3.70&Aring;
|PDB= 2hi7 |SIZE=350|CAPTION= <scene name='initialview01'>2hi7</scene>, resolution 3.70&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene>
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|LIGAND= <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi7 OCA], [http://www.ebi.ac.uk/pdbsum/2hi7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hi7 RCSB]</span>
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[[Category: Suzuki, M.]]
[[Category: Suzuki, M.]]
[[Category: Yamashita, E.]]
[[Category: Yamashita, E.]]
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[[Category: UQ1]]
 
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[[Category: ZN]]
 
[[Category: disulfide bond]]
[[Category: disulfide bond]]
[[Category: dsbb]]
[[Category: dsbb]]
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[[Category: ubiquinone]]
[[Category: ubiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:30:46 2008''

Revision as of 00:30, 31 March 2008


PDB ID 2hi7

Drag the structure with the mouse to rotate
, resolution 3.70Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of DsbA-DsbB-ubiquinone complex


Overview

Oxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial periplasmic space. DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic dithiol oxidase. To gain insight into disulfide bond formation, we determined the crystal structure of the DsbB-DsbA complex at 3.7 A resolution. The structure of DsbB revealed four transmembrane helices and one short horizontal helix juxtaposed with Cys130 in the mobile periplasmic loop. Whereas DsbB in the resting state contains a Cys104-Cys130 disulfide, Cys104 in the binary complex is engaged in the intermolecular disulfide bond and captured by the hydrophobic groove of DsbA, resulting in separation from Cys130. This cysteine relocation prevents the backward resolution of the complex and allows Cys130 to approach and activate the disulfide-generating reaction center composed of Cys41, Cys44, Arg48, and ubiquinone. We propose that DsbB is converted by its specific substrate, DsbA, to a superoxidizing enzyme, capable of oxidizing this extremely oxidizing oxidase.

About this Structure

2HI7 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation., Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, Ito K, Cell. 2006 Nov 17;127(4):789-801. PMID:17110337

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