Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.

@article{Fujiwara2005CrystalSO,
  title={Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.},
  author={Kazuko Fujiwara and Sachiko Toma and Kazuko Okamura-Ikeda and Yutaro Motokawa and Atsushi Nakagawa and Hisaaki Taniguchi},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 39},
  pages={33645-51}
}
Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal… CONTINUE READING