1a2m
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OXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM III
OverviewOverview
BACKGROUND: 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. RESULTS: We, have determined the crystal structures of reduced and oxidized DsbA in the, same crystal form and at the same pH (5.6). The crystal structure of a, lower pH form of oxidized DsbA has also been determined (pH 5.0). ... [(full description)]
About this StructureAbout this Structure
1A2M is a [Single protein] structure of sequence from [Escherichia coli]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization., Guddat LW, Bardwell JC, Martin JL, Structure. 1998 Jun 15;6(6):757-67. PMID:9655827
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