The topology of CuA in relation to the other metal centres in cytochrome-c oxidase of Saccharomyces cerevisiae as determined by analysis of second-site reversions
| Autor: | Peter R. Rich, Anne-Marie Colson, Brigitte Meunier |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Protein Conformation
Protein subunit Mutant Biophysics Saccharomyces cerevisiae Biology Ligands Topology Biochemistry Protein Structure Secondary Electron Transport Complex IV Suppression Genetic Protein structure Structural Biology Cytochrome c oxidase Binding site Molecular Biology Histidine Binding Sites Ligand digestive oral and skin physiology Mitochondria Mutation biology.protein Copper |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1253:13-15 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(95)92373-4 |
| Popis: | Second-site revertants were selected from a respiratory-deficient mutant carrying the mutation D369N located in a loop between helices IX and X close to H376 and H378, the proposed ligands of haem a(3) and haem a, respectively. A reversion was observed in subunit II, in the vicinity of the Cu-A ligands. This same reversion compensates the subunit I deficiency mutation, S140L, assumed to be near H62, the second putative histidine ligand to haem a. These data enable us to propose a three-dimensional topology in which Cu-A in subunit II is located on top of the Positive-side of subunit I and in proximity to all three of its metal centres. |
| Databáze: | OpenAIRE |
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