FEBS Letters
Volume 583, Issue 11 , Pages 1699-1702, 5 June 2009

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

Edited by Miguel De la Rosa

  • Lucia Banci

      Affiliations

    • Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
    • ,
  • Ivano Bertini

      Affiliations

    • Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
    • Corresponding Author InformationCorresponding author. Fax: +39 055 4574271.
    • ,
  • Simone Ciofi-Baffoni

      Affiliations

    • Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
    • ,
  • Kostas Tokatlidis

      Affiliations

    • Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology (IMBB-FORTH) and Department of Materials Science and Technology, University of Crete, Heraklion 70013, Crete, Greece

Received 16 March 2009; accepted 27 March 2009. published online 02 April 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.

Keywords: Coil-coiled helix, Redox

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(09)00257-9

doi:10.1016/j.febslet.2009.03.061

FEBS Letters
Volume 583, Issue 11 , Pages 1699-1702, 5 June 2009

Article Tools

* Image Usage & Resolution