Structural highlights
Function
[DSBC_HAEIN] Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial DsbC proteins are involved in rearranging or reducing mismatched disulfide bonds folding within the periplasm. The X-ray structure of the enzyme from Haemophilus influenzae has been solved and compared with the known structure of the Escherichia coli protein. The proteins act as V-shaped dimers with a large cleft to accommodate substrate proteins. The dimers are anchored by a small N-terminal domain, but have a flexible linker region which allows the larger C-terminal domain, with its reactive sulfhydryls, to clamp down on substrates. The overall folds are very similar, but the comparison shows a wider range of hinge motions than previously thought. The crystal packing of the H. influenzae protein allows the movement of the N-terminal domain with respect to the C-terminal domain through motions in the flexible hinge, generating high thermal parameters and unusually high anisotropy in the crystallographic data.
Structure of DsbC from Haemophilus influenzae.,Zhang M, Monzingo AF, Segatori L, Georgiou G, Robertus JD Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1512-8. Epub 2004, Aug 26. PMID:15333920[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang M, Monzingo AF, Segatori L, Georgiou G, Robertus JD. Structure of DsbC from Haemophilus influenzae. Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1512-8. Epub 2004, Aug 26. PMID:15333920 doi:10.1107/S0907444904014593
