1T3B

X-ray Structure of DsbC from Haemophilus influenzae

Summary for 1T3B

• Entry DOI: 10.2210/pdb1t3b/pdb
• Descriptor: Thiol:disulfide interchange protein dsbC (2 entities in total)
• Functional Keywords: oxidoreductase, protein disulfide isomerase, protein folding, redox protein, redox-active center, isomerase
• Biological source: Haemophilus influenzae
• Cellular location: Periplasm (By similarity): P45111
• Total number of polymer chains: 1
• Total formula weight: 23532.02

Authors

Zhang, M.,Monzingo, A.F.,Segatori, L.,Georgiou, G.,Robertus, J.D. (deposition date: 2004-04-26, release date: 2004-09-07, Last modification date: 2024-10-30)

Primary citation

Zhang, M.,Monzingo, A.F.,Segatori, L.,Georgiou, G.,Robertus, J.D.
Structure of DsbC from Haemophilus influenzae.
Acta Crystallogr.,Sect.D, 60:1512-1518, 2004

PubMed 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.

PubMed: 15333920
DOI: 10.1107/S0907444904014593

Experimental method

X-RAY DIFFRACTION (2.5 Å)