2ad7

crystal structure of methanol dehydrogenase from M. W3A1 (form C) in the presence of methanol

spinqualitylabelsall models 2ad7, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ad7 is a 4 chain structure with sequence from Methylophilus methylotrophus W3A1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: CA, PQQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DHM2_METME Catalyzes the oxidation of primary alcohols including methanol (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Methanol dehydrogenase is a heterotetrameric enzyme containing the prosthetic group pyrroloquinoline quinone (PQQ), which catalyzes the oxidation of methanol to formaldehyde. The crystal structure of methanol dehydrogenase from Methylophilus W3A1, previously determined at high resolution, exhibits a non-planar configuration of the PQQ ring system and lends support for a hydride transfer mechanism of the enzymatic reaction catalyzed by the enzyme. To investigate why PQQ is in the C5-reduced form and to better understand the catalytic mechanism of the enzyme, three structures of this enzyme in a new crystal form have been determined at higher resolution. Two of the three crystals were grown in the presence of 1 and 50 mM methanol, respectively, both structures of which show non-planar configurations of the PQQ ring system, confirming the previous conclusion; the other was crystallized in the presence of 50 mM ethanol, the structure of which displays a planar ring system for PQQ. Comparison of these structures reveals that the configuration change of PQQ is induced by the enzymatic reaction. The reaction takes place and the C5-reduced PQQ intermediate is produced when the enzyme co-crystallizes with methanol, but the enzymatic reaction does not take place and the PQQ ring retains a planar configuration of the oxidized orthoquinone form when ethanol instead of methanol is present in the crystallization solution. The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase.,Li J, Gan JH, Mathews FS, Xia ZX Biochem Biophys Res Commun. 2011 Mar 25;406(4):621-6. Epub 2011 Feb 26. PMID:21356200 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methanol dehydrogenase

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