| | The coiled coil-helix-coiled coil-helix proteins may be redox proteinsEdited by Miguel De la Rosa Received 16 March 2009; accepted 27 March 2009. published online 02 April 2009. 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. 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  Corresponding author. Fax: +39 055 4574271.
PII: S0014-5793(09)00257-9 doi:10.1016/j.febslet.2009.03.061 © 2009 Federation of European Biochemical Societies | |
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