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. © 2009 Federation of European Biochemical Societies.

The coiled coil-helix-coiled coil-helix proteins may be redox proteins / L.Banci; I.Bertini; S.Ciofi Baffoni; K.Tokatlidis. - In: FEBS LETTERS. - ISSN 0014-5793. - ELETTRONICO. - 11:(2009), pp. 1699-1702. [10.1016/j.febslet.2009.03.061]

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

BANCI, LUCIA;BERTINI, IVANO;CIOFI BAFFONI, SIMONE;
2009

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. © 2009 Federation of European Biochemical Societies.
2009
11
1699
1702
L.Banci; I.Bertini; S.Ciofi Baffoni; K.Tokatlidis
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/368684
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