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Title 

Crystal structure of DsbDγ reveals the mechanism of redox potential shift and substrate specificity

Authors 

Jae Hoon KimSeung-Jun KimDae Gwin JeongJeong Hee SonSeong Eon Ryu

Publisher 

Elsevier

Issue Date 

2003

Citation 

FEBS Letters, vol. 543, no. 1, pp. 164-169

Keywords 

crystal structureDsbDγelectron transferredox potentialthiol-disulfide exchange reactionprotein dsbd gammathioredoxinenzyme specificityoxidation reduction potentialstructure analysis

Abstract 

The Escherichia coli transmembrane protein DsbD transfers electrons from the cytoplasm to the periplasm through a cascade of thiol-disulfide exchange reactions. In this process, the C-terminal periplasmic domain of DsbD (DsbDγ) shuttles the reducing potential from the membrane domain (DsbDβ) to the N-terminal periplasmic domain (DsbDα). The crystal structure of DsbDγ determined at 1.9 ? resolution reveals that the domain has a thioredoxin fold with an extended N-terminal stretch. In comparison to thioredoxin, the DsbDγ structure exhibits the stabilized active site conformation and the extended active site α2 helix that explain the domain's substrate specificity and the redox potential shift, respectively. The hypothetical model of the DsbDγ:DsbDα complex based on the DsbDγ structure and previous structural studies indicates that the conserved hydrophobic residue in the C-X-X-C motif of DsbDγ may be important in the specific recognition of DsbDα.

ISSN 

0014-5793

Link 

http://dx.doi.org/10.1016/S0014-5793(03)00434-4

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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