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

Alexander Eletsky, Mi Young Jeong, Hyung Kim, Hsiau Wei Lee, Rong Xiao, David J. Pagliarini, James H. Prestegard, Dennis R. Winge, Gaetano T. Montelione, Thomas Szyperski

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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.

Original languageEnglish
Pages (from-to)8475-8477
Number of pages3
JournalBiochemistry
Volume51
Issue number43
DOIs
StatePublished - Oct 30 2012
Externally publishedYes

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