Abstract
The yeast mitochondrial protein Sdh5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a subunit of the heterotetrameric enzyme succinate dehydrogenase. The NMR structure of Sdh5 represents the first eukaryotic structure of Pfam family PF03937 and reveals a conserved surface region, which likely represents a putative Sdh1-Sdh5 interaction interface. Point mutations in this region result in the loss of covalent flavinylation of Sdh1. Moreover, chemical shift perturbation measurements showed that Sdh5 does not bind FAD in vitro, indicating that it is not a simple cofactor transporter in vivo.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Flavin-Adenine Dinucleotide / metabolism*
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Mitochondrial Proteins / chemistry*
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Mitochondrial Proteins / genetics
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Mitochondrial Proteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Point Mutation
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Protein Binding
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Protein Conformation
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Saccharomyces cerevisiae / chemistry*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Sequence Alignment
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Succinate Dehydrogenase / metabolism*
Substances
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Mitochondrial Proteins
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SDH1 protein, S cerevisiae
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SDH5 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Flavin-Adenine Dinucleotide
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Succinate Dehydrogenase