Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes.

@article{Lin2004SolutionSO,
  title={Solution structure of the 30 kDa polysulfide-sulfur transferase homodimer from Wolinella succinogenes.},
  author={Y Lin and Felician Dancea and Frank Loehr and Oliver Klimmek and Stefania Pfeiffer-Marek and Michael Nilges and Hans L J Wienk and Achim Kr{\"o}ger and Heinz R{\"u}terjans},
  journal={Biochemistry},
  year={2004},
  volume={43 6},
  pages={1418-24}
}
The periplasmic polysulfide-sulfur transferase (Sud) protein encoded by Wolinella succinogenes is involved in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The polysulfide-sulfur is covalently bound to the catalytic Cys residue of the Sud protein and transferred to the active site of the membranous polysulfide reductase. The solution structure of the homodimeric Sud protein has been determined using heteronuclear multidimensional NMR techniques. The… CONTINUE READING