The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues
| Autor: | A. Avezoux, Karl Harlos, Christopher Anthony, Colin C.F. Blake, Minakshi Ghosh |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Molecular Sequence Data Cofactor Electron Transport Electron transfer Structural Biology Amino Acid Sequence Cysteine Disulfides Molecular Biology chemistry.chemical_classification Binding Sites Gram-Negative Aerobic Bacteria Molecular Structure biology Methanol dehydrogenase Active site biology.organism_classification Quinone Alcohol Oxidoreductases Enzyme chemistry biology.protein Methylobacterium extorquens |
| Zdroj: | Nature Structural & Molecular Biology. 1:102-105 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsb0294-102 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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