1t3b
X-ray Structure of DsbC from Haemophilus influenzae
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OverviewOverview
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.
About this StructureAbout this Structure
1T3B is a Single protein structure of sequence from Haemophilus influenzae. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.
ReferenceReference
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
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