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Biochemistry. 2012 Oct 30;51(43):8475-7. doi: 10.1021/bi301171u. Epub 2012 Oct 19.

Solution NMR structure of yeast succinate dehydrogenase flavinylation factor Sdh5 reveals a putative Sdh1 binding site.

Author information

1
Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.

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.

PMID:
23062074
PMCID:
PMC3667956
DOI:
10.1021/bi301171u
[Indexed for MEDLINE]
Free PMC Article
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