2i4a
Crystal structure of thioredoxin from the acidophile Acetobacter aceti
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OverviewOverview
The crystal structure of thioredoxin (AaTrx) from the acetic acid, bacterium Acetobacter aceti was determined at 1 A resolution. This is, currently the highest resolution crystal structure available for any, thioredoxin. Thioredoxins facilitate thiol-disulfide exchange, a process, that is expected to be slow at the low pH values encountered in the A., aceti cytoplasm. Despite the apparent need to function at low pH, neither, the active site nor the surface charge distribution of AaTrx is notably, different from that of Escherichia coli thioredoxin. Apparently the, ancestral thioredoxin was sufficiently stable for use in A. aceti or the, need to interact with multiple targets constrained the variation of, surface residues. The AaTrx structure presented here provides a clear view, of all ionizable protein moieties and waters, a first step in, understanding how thiol-disulfide exchange might occur in a low pH, cytoplasm, and is a basis for biophysical studies of the mechanism of, acid-mediated unfolding. The high resolution of this structure should be, useful for computational studies of thioredoxin function, protein, structure and dynamics, and side-chain ionization.
About this StructureAbout this Structure
2I4A is a Protein complex structure of sequences from Acetobacter aceti with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti., Starks CM, Francois JA, MacArthur KM, Heard BZ, Kappock TJ, Protein Sci. 2007 Jan;16(1):92-8. PMID:17192591
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