Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site.

@article{Singh2014StructuresOT,
  title={Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site.},
  author={Harkewal Singh and Benjamin W. Arentson and Donald F Becker and John J. Tanner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 9},
  pages={3389-94}
}
Proline utilization A (PutA) proteins are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of L-proline to L-glutamate by the sequential activities of proline dehydrogenase and aldehyde dehydrogenase domains. Located at the inner membrane of Gram-negative bacteria, PutAs play a major role in energy metabolism by coupling the oxidation of proline imported from the environment to the reduction of membrane-associated quinones. Here, we report seven crystal structures of… CONTINUE READING
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