The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens.
The crystal structure of methanol dehydrogenase (MDH) from Methylobacterium extorquens has been refined without stereochemical restraints at a resolution of 1.2 A. 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 quinohaemo-protein 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.
Williams
P A
PA
School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, England.
Coates
L
L
Mohammed
F
F
Gill
R
R
Erskine
P T
PT
Coker
A
A
Wood
S P
SP
Anthony
C
C
Cooper
J B
JB
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry; D004583:Electrons; D020601:Methylobacterium extorquens / Q000201:enzymology*; D008958:Models, Molecular; D008962:Models, Theoretical; D045542:PQQ Cofactor / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011522:Protons
D003574:Cytochrome c Group; D011522:Protons; D045542:PQQ Cofactor; C058498:cytochrome C(L); D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C019641:alcohol dehydrogenase (acceptor); D002118:Calcium