Cytochrome c oxidase assembly process involves many accessory proteins including Cox11, which is a copper-binding protein required for Cu incorporation into the CuB site of cytochrome c oxidase. In a genome wide search, a number of Cox11 homologs are found in all of the eukaryotes with complete genomes and in several Gram-negative bacteria. All of them possess a highly homologous soluble domain and contain an N-terminal fragment that anchors the protein to the membrane. An anchor-free construct of 164 amino acids was obtained from Sinorhizobium meliloti, and the first structure of this class of proteins is reported here. The apoform has an immunoglobulin-like fold with a novel type of β-strand organization. The copper binding motif composed of two highly conserved cysteines is located on one side of the β-barrel structure. The apoprotein is monomeric in the presence of dithiothreitol, whereas it dimerizes in the absence of the reductant. When copper(I) binds, NMR and extended x-ray absorption fine structure (EXAFS) data indicate a dimeric protein state with two thiolates bridging two copper(I) ions. The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly.
Solution Structure of Cox11, a Novel Type of β-Immunoglobulin-like Fold Involved in CuB Site Formation of Cytochrome c Oxidase*
L. Banci,I. Bertini,F. Cantini,S. Ciofi‐Baffoni,L. Gonnelli,S. Mangani
Published 2004 in Journal of Biological Chemistry
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- Publication year
2004
- Venue
Journal of Biological Chemistry
- Publication date
2004-08-13
- Fields of study
Biology, Medicine, Materials Science, Chemistry
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Semantic Scholar, PubMed
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