The active site structure of the calcium-containing quinoprotein methanol dehydrogenase

Pyrroloquinoline quinone (PQQ), widely found in nature, serves as the redox cofactor in bacterial methanol dehydrogenase (MEDH), a heterotetrameric enzyme that oxidizes methanol to formaldehyde. The refined structure of MEDH at 2.4-A resolution, based on recently obtained amino acid sequence data, r...

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Bibliographic Details
Published in:Biochemistry (Easton) 1993-12, Vol.32 (48), p.12955-12958
Main Authors: White, Scott, Boyd, Geoffrey, Mathews, F. Scott, Xia, Zongxiang, Dai, Weiwen, Zhang, Yuefan, Davidson, Victor L.
Format: Article
Language:English
Subjects:
Alcohol Oxidoreductases - ultrastructure
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Bacterial Proteins - ultrastructure
Binding Sites
Biological and medical sciences
Calcium-Binding Proteins - ultrastructure
Crystalline structure
Crystallography, X-Ray
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Gram-Negative Bacteria - enzymology
Hydrogen Bonding
Methylophilus
Models, Molecular
Molecular biophysics
Molecular Sequence Data
Oxidoreductases
PQQ Cofactor
Protein Structure, Tertiary
Quinolones - chemistry
Structure in molecular biology
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Summary:Pyrroloquinoline quinone (PQQ), widely found in nature, serves as the redox cofactor in bacterial methanol dehydrogenase (MEDH), a heterotetrameric enzyme that oxidizes methanol to formaldehyde. The refined structure of MEDH at 2.4-A resolution, based on recently obtained amino acid sequence data, reveals that the PQQ, located in a central channel of the disk-shaped protein, is sandwiched between a Trp side chain and a very unusual vicinal disulfide. A Ca2+ ion forms a bridge between PQQ and the protein molecule, very close to a putative substrate binding pocket. The vicinal disulfide may form during PQQ incorporation and possibly act to hold the latter in place.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00211a002