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The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues

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An Erratum to this article was published on 01 August 1994

Abstract

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.

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, UK

    C.C.F. Blake, M. Ghosh & K. Harlos

  2. SERC Centre for Molecular Recognition, Department of Biochemistry, University of Southampton, UK

    A. Avezoux & C. Anthony

Authors
  1. C.C.F. Blake
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  2. M. Ghosh
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  3. K. Harlos
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  4. A. Avezoux
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  5. C. Anthony
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Blake, C., Ghosh, M., Harlos, K. et al. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat Struct Mol Biol 1, 102–105 (1994). https://doi.org/10.1038/nsb0294-102

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