1G72

CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION

Replaces:  1B2N

Summary for 1G72

• Entry DOI: 10.2210/pdb1g72/pdb
• Related: 4AAH
• Descriptor: METHANOL DEHYDROGENASE HEAVY SUBUNIT, METHANOL DEHYDROGENASE LIGHT SUBUNIT, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: quinoprotein, oxidoreductase
• Biological source: Methylophilus methylotrophus; More
• Cellular location: Cell inner membrane; Peripheral membrane protein; Periplasmic side: P38539 P38540
• Total number of polymer chains: 4
• Total formula weight: 141687.50

Authors

Zheng, Y.,Xia, Z.,Chen, Z.,Bruice, T.C.,Mathews, F.S. (deposition date: 2000-11-08, release date: 2001-01-24, Last modification date: 2024-11-20)

Primary citation

Zheng, Y.J.,Xia, Z.x.,Chen, Z.w.,Mathews, F.S.,Bruice, T.C.
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation.
Proc.Natl.Acad.Sci.USA, 98:432-434, 2001

PubMed Abstract: The catalytic mechanism of the reductive half reaction of the quinoprotein methanol dehydrogenase (MDH) is believed to proceed either through a hemiketal intermediate or by direct transfer of a hydride ion from the substrate methyl group to the cofactor, pyrroloquinoline quinone (PQQ). A crystal structure of the enzyme-substrate complex of a similar quinoprotein, glucose dehydrogenase, has recently been reported that strongly favors the hydride transfer mechanism in that enzyme. A theoretical analysis and an improved refinement of the 1.9-A resolution crystal structure of MDH from Methylophilus methylotrophus W3A1 in the presence of methanol, reported earlier, indicates that the observed tetrahedral configuration of the C-5 atom of PQQ in that study represents the C-5-reduced form of the cofactor and lends support for a hydride transfer mechanism for MDH.

PubMed: 11149955
DOI: 10.1073/pnas.021547498

Experimental method

X-RAY DIFFRACTION (1.9 Å)