1srx
|
THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION
OverviewOverview
The three-dimensional structure of the electron transport protein, thioredoxin-S2 from E. coli has been determined from a 2.8 A resolution, electron density map. The molecule is built up of a central core of three, parallel and two antiparallel strands of pleated sheet surrounded by four, helices. Thr residues involved in the active center 14-membered disulfide, ring of thioredoxin form a protrusion between one of the helices and the, middle strand of the pleated sheet. This region of the molecule, comprising two parallel strands joined by the protrusion and a helix, is, structurally very similar to corresponding functionally important regions, in the nucleotide-binding domains of flavodoxin and the dehydrogenases., The molecule has about 75% of the residues in well-defined secondary, structures. The structure indicates that the carboxy-terminal third of the, molecule forms an independent folding unit consisting of two strands of, antiparallel pleated sheet and a terminal alpha-helix. This agress with, the noncovalent reconstitution experiments from thioredoxin peptide, fragments. Thioredoxin is an example of a protein with the active center, located on a protrusion rather than in a cleft, thus demonstrating the, existence of male proteins.
About this StructureAbout this Structure
1SRX is a Single protein structure of sequence from Escherichia coli b. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution., Holmgren A, Soderberg BO, Eklund H, Branden CI, Proc Natl Acad Sci U S A. 1975 Jun;72(6):2305-9. PMID:1094461
Page seeded by OCA on Wed Nov 21 02:36:56 2007