Journal
FEBS LETTERS
Volume 583, Issue 11, Pages 1699-1702Publisher
WILEY
DOI: 10.1016/j.febslet.2009.03.061
Keywords
Coil-coiled helix; Redox
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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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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