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The coiled coil-helix-coiled coil-helix proteins may be redox proteins |
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| Authors: | Lucia Banci Simone Ciofi-Baffoni |
| Affiliation: | a Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy b Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology (IMBB-FORTH) and Department of Materials Science and Technology, University of Crete, Heraklion 70013, Crete, Greece |
| Abstract: | A number of nuclear encoded proteins are imported in to the intermembrane space of mitochondria where they adopt a coiled coil-helix-coiled coil-helix (CHCH) fold. Two disulfide bonds formed by twin CX3C or CX9C motifs stabilize this fold. Some of these proteins are also characterized at their N-termini by the presence of two additional cysteine residues which can perform oxidoreductase or metallochaperone functions or both. This fold represents the most ‘minimal’ oxidoreductase domain described so far. |
| Keywords: | Coil-coiled helix Redox |
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