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Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy

Academic Article
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Overview

authors

  • Dyson, Jane
  • Gippert, Garry
  • Case, David A.
  • Holmgren, A.
  • Wright, Peter

publication date

  • May 1990

journal

  • Biochemistry  Journal

abstract

  • The three-dimensional solution structure of reduced (dithiol) thioredoxin from Escherichia coli has been determined with distance and dihedral angle constraints obtained from 1H NMR spectroscopy. Reduced thioredoxin has a well-defined global fold consisting of a central five-strand beta-sheet and three long helices. The beta-strands are packed in the sheet in the order beta 1 beta 3 beta 2 beta 4 beta 5, with beta 1, beta 3, and beta 2 parallel and beta 2, beta 4, and beta 5 arranged in an antiparallel fashion. Two of the helices connect strands of the beta-sheet: alpha 1 between beta 1 and beta 2 and alpha 2 between beta 2 and beta 3. Strands beta 4 and beta 5 are connected by a short loop that contains a beta-bulge. Strands beta 3 and beta 4 are connected by a long loop that contains a series of turn-like or 3(10) helical structures. The active site Cys-Gly-Pro-Cys sequence forms a protruding loop between strand beta 2 and helix alpha 2. The structure is very similar overall to that of oxidized (disulfide) thioredoxin obtained from X-ray crystal structure analysis but differs in the local conformation of the active site loop. The distance between the sulfurs of Cys 32 and Cys 35 increases from 2.05 A in the disulfide bridge to 6.8 +/- 0.6 A in the dithiol of reduced thioredoxin, as a result of a rotation of the side chain of Cys 35 and a significant change in the position of Pro 34. This conformational change has important implications for the mechanism of thioredoxin as a protein disulfide oxidoreductase.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Binding Sites
  • Disulfides
  • Escherichia coli
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Conformation
  • Thioredoxins
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00469a016

PubMed ID

  • 2193685
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Additional Document Info

start page

  • 4129

end page

  • 4136

volume

  • 29

issue

  • 17

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