title: High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin.
abstract: BACKGROUND
  Thioredoxin participates in thiol-disulfide exchange reactions and both oxidized thioredoxin (disulfide form) and reduced thioredoxin (dithiol form) are found under physiological conditions. Previous structural studies suggested that the two forms were extremely similar, although significant functional and spectroscopic differences exist. We therefore undertook high-resolution solution structural studies of the two forms of Escherichia coli thioredoxin in order to detect subtle conformational differences.
  
  
  RESULTS
  The solution structures of reduced and oxidized thioredoxin are extremely similar. Backbone structure is largely identical in the two forms, with slight differences in the region of the active site, which includes Cys32 and Cys35. The side chain sulfur atom of Cys32 is tilted away from that of Cys35 in the reduced form of the protein to accommodate the increase in S-S distance that occurs upon reduction of the disulfide, but the chi 1 angles of the two cysteines remain the same in the two forms.
  
  
  CONCLUSIONS
  Only subtle conformational changes occur upon changing the oxidation state of the active site cysteines, including the positions of some side chains and in hydrogen bonding patterns in the active site region. Functional differences between the two forms are probably therefore related to differences in local conformational flexibility in and near the active site loop.
authors: Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
authors: M F
authors: MF
authors: Jeng
authors: A P
authors: AP
authors: Campbell
authors: T
authors: T
authors: Begley
authors: A
authors: A
authors: Holmgren
authors: D A
authors: DA
authors: Case
authors: P E
authors: PE
authors: Wright
authors: H J
authors: HJ
authors: Dyson
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D012996:Solutions; D013879:Thioredoxins