Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor.

@article{Shibata2005ReleaseOA,
  title={Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor.},
  author={Naoki Shibata and Koichi Mori and Naoki Hieda and Yoshiki Higuchi and Mamoru Yamanishi and Tetsuo Toraya},
  journal={Structure},
  year={2005},
  volume={13 12},
  pages={1745-54}
}
The crystal structures of ADP bound and nucleotide-free forms of molecular chaperone-like diol dehydratase-reactivating factor (DDR) were determined at 2.0 and 3.0 A, respectively. DDR exists as a dimer of heterodimer (alphabeta)2. The alpha subunit has four domains: ATPase domain, swiveling domain, linker domain, and insert domain. The beta subunit, composed of a single domain, has a similar fold to the beta subunit of diol dehydratase (DD). The binding of an ADP molecule to the nucleotide… CONTINUE READING

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