Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution.

@article{Xia1999DetailedAS,
  title={Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution.},
  author={Z X Xia and Yanping He and Wei Wei Dai and Scott A White and Gary D Boyd and F. Scott Mathews},
  journal={Biochemistry},
  year={1999},
  volume={38 4},
  pages={1214-20}
}
The three-dimensional structure of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 has been obtained in the presence of substrate using data recorded at a synchrotron. The structure of this approximately 140 kDa heterotetramer, refined at 1. 9 A resolution, reveals the detailed configuration of its redox cofactor, pyrroloquinoline quinone (PQQ). C4, one of the oxygen-bearing atoms of this orthoquinone is in a planar configuration while C5, which bears the other quinone… CONTINUE READING

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