| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2050207 | FEBS Letters | 2009 | 4 Pages |
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.
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Authors
Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Kostas Tokatlidis,