Structure of DsbC from Haemophilus influenzae.
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.
Zhang
Man
M
Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, 1 University Station, University of Texas at Austin, Austin, TX 78712, USA.
Monzingo
Arthur F
AF
Segatori
Laura
L
Georgiou
George
G
Robertus
Jon D
JD
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
D019704:Protein Disulfide-Isomerases