1W6S

The high resolution structure of methanol dehydrogenase from methylobacterium extorquens

Summary for 1W6S

• Entry DOI: 10.2210/pdb1w6s/pdb
• Related: 1H4I 1H4J
• Descriptor: METHANOL DEHYDROGENASE SUBUNIT 1, METHANOL DEHYDROGENASE SUBUNIT 2, PYRROLOQUINOLINE QUINONE, ... (6 entities in total)
• Functional Keywords: anisotropic, electron transfer, oxidoreductase, calcium-binding, methanol utilization, pqq
• Biological source: METHYLOBACTERIUM EXTORQUENS; More
• Total number of polymer chains: 4
• Total formula weight: 149655.71

Authors

Williams, P.A.,Coates, L.,Mohammed, F.,Gill, R.,Erskine, P.T.,Wood, S.P.,Anthony, C.,Cooper, J.B. (deposition date: 2004-08-23, release date: 2004-12-21, Last modification date: 2024-11-13)

Primary citation

Williams, P.A.,Coates, L.,Mohammed, F.,Gill, R.,Erskine, P.T.,Wood, S.P.,Anthony, C.,Cooper, J.B.
The Atomic Resolution Structure of Methanol Dehydrogenase from Methylobacterium Extorquens
Acta Crystallogr.,Sect.D, 61:75-, 2005

PubMed Abstract: 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.

PubMed: 15608378
DOI: 10.1107/S0907444904026964

Experimental method

X-RAY DIFFRACTION (1.2 Å)