1jpe
|
Crystal structure of DsbD-alpha; the N-terminal domain of DsbD
OverviewOverview
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect, disulfide bonds during oxidative protein folding. It is specifically, activated by the periplasmic N-terminal domain (DsbDalpha) of the, transmembrane electron transporter DsbD. An intermediate of the electron, transport reaction was trapped, yielding a covalent DsbC-DsbDalpha, complex. The 2.3 A crystal structure of the complex shows for the first, time the specific interactions between two thiol oxidoreductases., DsbDalpha is a novel thiol oxidoreductase with the active site cysteines, embedded in an immunoglobulin fold. It binds into the central cleft of the, V-shaped DsbC dimer, which assumes a closed conformation on complex, formation. Comparison of the complex with oxidized DsbDalpha reveals major, conformational changes in a cap structure that regulates the accessibility, of the DsbDalpha active site. Our results explain how DsbC is selectively, activated by DsbD using electrons derived from the cytoplasm.
About this StructureAbout this Structure
1JPE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex., Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P, EMBO J. 2002 Sep 16;21(18):4774-84. PMID:12234918
Page seeded by OCA on Tue Nov 20 18:27:15 2007