The coiled coil-helix-coiled coil-helix proteins may be redox proteins

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 > Institute of Molecular Cell and Systems Biology
Journal Name:FEBS Letters
Publisher:Elsevier
ISSN:0014-5793
ISSN (Online):1873-3468

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