title: Structure of DsbC from Haemophilus influenzae.
abstract: 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.
authors.affiliation: Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, 1 University Station, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Man
authors.initials: M
authors.lastname: Zhang
authors.forename: Arthur F
authors.initials: AF
authors.lastname: Monzingo
authors.forename: Laura
authors.initials: L
authors.lastname: Segatori
authors.forename: George
authors.initials: G
authors.lastname: Georgiou
authors.forename: Jon D
authors.initials: JD
authors.lastname: Robertus
mesh_terms: D016880:Anisotropy; D003460:Crystallization; D018360:Crystallography, X-Ray; D006193:Haemophilus influenzae / Q000737:chemistry*; D008958:Models, Molecular; D019704:Protein Disulfide-Isomerases / Q000737:chemistry*; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D019704:Protein Disulfide-Isomerases