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The coiled coil‐helix‐coiled coil‐helix proteins may be redox proteins
Author(s) -
Banci Lucia,
Bertini Ivano,
Ciofi-Baffoni Simone,
Tokatlidis Kostas
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.061
Subject(s) - coiled coil , helix (gastropod) , chemistry , electromagnetic coil , biophysics , biochemistry , biology , physics , ecology , snail , quantum mechanics
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 CX 3 C or CX 9 C 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.