Solution structure of Grx4, a monothiol glutaredoxin from E. coli.
Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.
MSTTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALAACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGEL VGGCDIVIEMYQRGELQQLIKETAAKYKSEEPDAE
The structure was determined using triple-resonance NMR spectroscopy
The structures are based on 2703 NOE-DERIVED distance constraints, 77 J coupling derived dihedral angle restraints, 164 backbone torsion angle restraints derived from chemical shifts
0.8mM Grx4 U,15N,15N-13C; 5mM phopsphate, 125mM KCl
Mixed alpha/beta fold, Thioredoxin fold, Electron Transport