1w6s

From Proteopedia

Revision as of 15:22, 5 November 2007

THE HIGH RESOLUTION STRUCTURE OF METHANOL DEHYDROGENASE FROM METHYLOBACTERIUM EXTORQUENS

Overview

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.

About this Structure

1W6S is a Protein complex structure of sequences from Methylobacterium extorquens with CA, PQQ and GOL as ligands. Active as Alcohol dehydrogenase (acceptor), with EC number 1.1.99.8 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens., Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):75-9. Epub 2004 Dec, 17. PMID:15608378

Page seeded by OCA on Mon Nov 5 17:27:31 2007