1A2M

OXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM III

Summary for 1A2M

• Entry DOI: 10.2210/pdb1a2m/pdb
• Descriptor: DISULFIDE BOND FORMATION PROTEIN (2 entities in total)
• Functional Keywords: oxidoreductase, protein disulfide isomerase, protein folding, redox protein, redox-active center
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 42310.05

Authors

Martin, J.L.,Guddat, L.W. (deposition date: 1998-01-06, release date: 1998-07-08, Last modification date: 2024-10-30)

Primary citation

Guddat, L.W.,Bardwell, J.C.,Martin, J.L.
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.
Structure, 6:757-767, 1998

PubMed Abstract: The redox proteins that incorporate a thioredoxin fold have diverse properties and functions. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. In the domain motion model, hinge bending between the two domains of DsbA occurs as a result of redox-related conformational changes.

PubMed: 9655827
DOI: 10.1016/S0969-2126(98)00077-X

Experimental method

X-RAY DIFFRACTION (2.7 Å)