1. Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans
- Author
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Ben Prickril, Larry C. Sieker, Lyle H. Jensen, Ronald E. Stenkamp, and Jean LeGall
- Subjects
Models, Molecular ,Protein Conformation ,Biophysics ,Crystal structure ,Biochemistry ,X-Ray Diffraction ,Structural Biology ,Rubredoxin ,Genetics ,Molecule ,Amino Acids ,Molecular Biology ,Histidine ,biology ,Chemistry ,Rubredoxins ,Tryptophan ,Cell Biology ,Desulfovibrio desulfuricans ,biology.organism_classification ,Crystallography ,Ferredoxins ,Desulfovibrio ,Rubredoxin Fe-protein Histidine Sulfhydryl group Crystallography Electron transport ,Bacteria ,Cysteine - Abstract
The X-ray crystallographic structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 is described. This molecule is 15% smaller than previously studied rubredoxins, lacking a seven-residue loop of chain but containing a histidine and a free-sulfhydryl cysteine. Except for solvent exposure of the single invariant tryptophan, no other major difference occurs in the molecule.
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