2LM4

Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium Target YT682A

2LM4 の概要

• エントリーDOI: 10.2210/pdb2lm4/pdb
• NMR情報: BMRB: 18098
• 分子名称: Succinate dehydrogenase assembly factor 2, mitochondrial (1 entity in total)
• 機能のキーワード: structural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, protein binding, mitochondrial protein partnership, mpp
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Mitochondrion matrix: Q08230
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13193.03

構造登録者

Eletsky, A.,Winge, D.R.,Lee, H.,Lee, D.,Kohan, E.,Hamilton, K.,Acton, T.B.,Xiao, R.,Everett, J.K.,Prestegard, J.H.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG),Mitochondrial Protein Partnership (MPP) (登録日: 2011-11-22, 公開日: 2012-01-04, 最終更新日: 2024-05-15)

主引用文献

Eletsky, A.,Jeong, M.Y.,Kim, H.,Lee, H.W.,Xiao, R.,Pagliarini, D.J.,Prestegard, J.H.,Winge, D.R.,Montelione, G.T.,Szyperski, T.
Solution NMR structure of yeast succinate dehydrogenase flavinylation factor sdh5 reveals a putative sdh1 binding site.
Biochemistry, 51:8475-8477, 2012

PubMed 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.

PubMed: 23062074
DOI: 10.1021/bi301171u

実験手法

SOLUTION NMR