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2hi7

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{{STRUCTURE_2hi7| PDB=2hi7 | SCENE= }}
{{STRUCTURE_2hi7| PDB=2hi7 | SCENE= }}
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'''Crystal structure of DsbA-DsbB-ubiquinone complex'''
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===Crystal structure of DsbA-DsbB-ubiquinone complex===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17110337 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17110337}}
==About this Structure==
==About this Structure==
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[[Category: Redox]]
[[Category: Redox]]
[[Category: Ubiquinone]]
[[Category: Ubiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:19:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:13:10 2008''

Revision as of 05:13, 29 July 2008

Template:STRUCTURE 2hi7

Crystal structure of DsbA-DsbB-ubiquinone complex

Template:ABSTRACT PUBMED 17110337

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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