The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.
Adjacent cysteine residues can only form disulphide bridges in a distorted structure containing a cis-peptide link. Such bridges are extremely uncommon, identified so far in the acetyl choline receptor alone where the structure of the bridge is undetermined. Here we present the first molecular description of a disulphide bridge of this type in the quinoprotein methanol dehydrogenase from Methylobacterium extorquens. We show that this structure occurs in close proximity to the pyrrolo-quinoline quinone prosthetic group and a calcium ion in the active site of the enzyme. This unusual disulphide bridge appears to play a role in the electron transfer reaction mediated by methanol dehydrogenase.
Blake
C C
CC
Laboratory of Molecular Biophysics, University of Oxford, UK.
Ghosh
M
M
Harlos
K
K
Avezoux
A
A
Anthony
C
C
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D004579:Electron Transport; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation
D004220:Disulfides; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor); D003545:Cysteine