1SRX

THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION

Summary for 1SRX

• Entry DOI: 10.2210/pdb1srx/pdb
• Descriptor: THIOREDOXIN (1 entity in total)
• Functional Keywords: electron transport
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 11759.45

Authors

Soderberg, B.-O. (deposition date: 1976-05-06, release date: 1976-05-19, Last modification date: 2024-02-14)

Primary citation

Holmgren, A.,Soderberg, B.O.,Eklund, H.,Branden, C.I.
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.
Proc.Natl.Acad.Sci.USA, 72:2305-2309, 1975

PubMed Abstract: 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.

PubMed: 1094461
DOI: 10.1073/pnas.72.6.2305

Experimental method

X-RAY DIFFRACTION (2.8 Å)