Banci, L., Bertini, I., Ciofi-Baffoni, S. and Tokatlidis, K. (2009) The coiled coil-helix-coiled coil-helix proteins may be redox proteins. FEBS Letters, 583(11), pp. 1699-1702. (doi: 10.1016/j.febslet.2009.03.061)
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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.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Tokatlidis, Professor Kostas |
| Authors: | Banci, L., Bertini, I., Ciofi-Baffoni, S., and Tokatlidis, K. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
| Journal Name: | FEBS Letters |
| Publisher: | Elsevier |
| ISSN: | 0014-5793 |
| ISSN (Online): | 1873-3468 |
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