| Literature DB >> 19345215 |
Lucia Banci1, Ivano Bertini, Simone Ciofi-Baffoni, Kostas Tokatlidis.
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 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.Entities:
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Year: 2009 PMID: 19345215 DOI: 10.1016/j.febslet.2009.03.061
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124