Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation

Kenji Inaba, Satoshi Murakami, Mamoru Suzuki, Atsushi Nakagawa, Eiki Yamashita, Kengo Okada, Koreaki Ito

Research output: Contribution to journalArticlepeer-review

203 Citations (Scopus)


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 Å 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.

Original languageEnglish
Pages (from-to)789-801
Number of pages13
Issue number4
Publication statusPublished - 2006 Nov 17


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