The structure of a reduced mutant T4 glutaredoxin

FEBS Lett. 1995 Aug 21;370(3):209-11. doi: 10.1016/0014-5793(95)00806-k.

Abstract

The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure. The main differences are seen around the active site where the sulfurs of Cys14 and Cys17 move apart slightly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage T4 / chemistry
  • Bacteriophage T4 / genetics*
  • Crystallography
  • Glutaredoxins
  • Mutation
  • Oxidoreductases*
  • Proline / chemistry
  • Proline / genetics
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / genetics*
  • Tyrosine / chemistry
  • Tyrosine / genetics
  • Valine / chemistry
  • Valine / genetics

Substances

  • Glutaredoxins
  • Proteins
  • Tyrosine
  • Proline
  • Oxidoreductases
  • Valine