A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex.

@article{Kato2006ASS,
  title={A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex.},
  author={Masato Kato and R. Max Wynn and Jacinta L. Chuang and Chad A. Brautigam and Myra Custorio and David T Chuang},
  journal={The EMBO journal},
  year={2006},
  volume={25 24},
  pages={5983-94}
}
The dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex forms a cubic scaffold that catalyzes acyltransfer from S-acyldihydrolipoamide to CoA to produce acyl-CoA. We have determined the first crystal structures of a mammalian (bovine) E2b core domain with and without a bound CoA or acyl-CoA. These structures reveal both hydrophobic and the previously unreported ionic interactions between two-fold-related trimers that build up the cubic… CONTINUE READING

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