Open AccessThe atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens
Author(s) -
Williams P. A.,
Coates L.,
Mohammed F.,
Gill R.,
Erskine P. T.,
Coker A.,
Wood S. P.,
Anthony C.,
Cooper J. B.
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904026964
Subject(s) - methanol dehydrogenase , pyrroloquinoline quinone , comamonas testosteroni , chemistry , stereochemistry , cofactor , electron acceptor , active site , oxidoreductase , alcohol oxidoreductase , electron transfer , methanol , biochemistry , enzyme , nad+ kinase , photochemistry , organic chemistry
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 c L . A pathway for proton transfer from the active site to the bulk solvent is also suggested.