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The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens

By P.A. Williams, L. Coates, F. Mohammed, R. Gill, P.T. Erskine, A. Coker, S.P. Wood, C. Anthony and J.B. Cooper


The crystal structure of methanol dehydrogenase (MDH) from Methylobacterium extorquens has been refined without stereochemical restraints at a resolution of 1.2 Å. The high-resolution data have defined the conformation of the tricyclic pyrroloquinoline quinone (PQQ) cofactor ring as entirely planar. The detailed definition of the active-site geometry has shown many features that are similar to the quinohaemoprotein alcohol dehydrogenases from Comamonas testosteroni and Pseudomonas putida, both of which possess MDH-like and cytochrome c-like domains. Conserved features between the two types of PQQ-containing enzyme suggest a common pathway for electron transfer between MDH and its physiological electron acceptor cytochrome cL. A pathway for proton transfer from the active site to the bulk solvent is also suggested

Topics: QH301
Year: 2005
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Provided by: e-Prints Soton
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