rdf:type |
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lifeskim:mentions |
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pubmed:issue |
34
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pubmed:dateCreated |
2002-8-19
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pubmed:abstractText |
Cox11 is a protein essential for respiratory growth and has been implicated in the assembly of the Cu(B) site of cytochrome c oxidase. In the present study, we demonstrate that Cox11 is a copper-binding protein. The soluble C-terminal domain of Cox11 forms a dimer that coordinates one Cu(I) per monomer via three thiolate ligands. The two Cu(I) ions in the dimer exist in a binuclear cluster and appear to be ligated by three conserved Cys residues. Mutation of any of these Cys residues reduces Cu(I) binding and confers respiratory incompetence. Cytochrome c oxidase activity is reduced in these mutants. Thus, the residues important for Cu(I) binding correlate with in vivo function, suggesting that Cu(I) binding is important in Cox11 function.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31237-42
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12063264-Amino Acid Sequence,
pubmed-meshheading:12063264-Binding Sites,
pubmed-meshheading:12063264-Carrier Proteins,
pubmed-meshheading:12063264-Copper,
pubmed-meshheading:12063264-Cysteine,
pubmed-meshheading:12063264-Dimerization,
pubmed-meshheading:12063264-Electron Transport Complex IV,
pubmed-meshheading:12063264-Membrane Proteins,
pubmed-meshheading:12063264-Mitochondrial Proteins,
pubmed-meshheading:12063264-Molecular Sequence Data,
pubmed-meshheading:12063264-Protein Biosynthesis,
pubmed-meshheading:12063264-Protein Conformation,
pubmed-meshheading:12063264-Saccharomyces cerevisiae Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein.
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pubmed:affiliation |
University of Utah Health Sciences Center, Salt Lake City, UT 84132, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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