4IHU

Reduced form of disulfide bond oxdioreductase (DsbG) from Mycobacterium tuberculosis

Summary for 4IHU

• Entry DOI: 10.2210/pdb4ihu/pdb
• Descriptor: Isomerase DsbG, CHLORIDE ION (3 entities in total)
• Functional Keywords: thioredoxin, disulfide bond isomerase, redox, oxidoreductase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 47285.93

Authors

Harmston, C.A.,Goulding, C.W. (deposition date: 2012-12-19, release date: 2013-10-30, Last modification date: 2024-11-20)

Primary citation

Chim, N.,Harmston, C.A.,Guzman, D.J.,Goulding, C.W.
Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis.
Bmc Struct.Biol., 13:23-23, 2013

PubMed Abstract: Bacterial Disulfide bond forming (Dsb) proteins facilitate proper folding and disulfide bond formation of periplasmic and secreted proteins. Previously, we have shown that Mycobacterium tuberculosis Mt-DsbE and Mt-DsbF aid in vitro oxidative folding of proteins. The M. tuberculosis proteome contains another predicted membrane-tethered Dsb protein, Mt-DsbA, which is encoded by an essential gene.

PubMed: 24134223
DOI: 10.1186/1472-6807-13-23

Experimental method

X-RAY DIFFRACTION (1.896 Å)