Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site

被引：25

作者：

Eletsky, Alexander ^{[1
]}

Jeong, Mi-Young ^{[2
,3
]}

Kim, Hyung ^{[2
,3
]}

Lee, Hsiau-Wei ^{[4
]}

Xiao, Rong ^{[5
,6
,7
]}

Pagliarini, David J. ^{[8
]}

Prestegard, James H. ^{[4
]}

Winge, Dennis R. ^{[2
,3
]}

Montelione, Gaetano T. ^{[5
,6
,7
]}

Szyperski, Thomas ^{[1
]}

机构：

[1] SUNY Buffalo, Dept Chem, Buffalo, NY 14260 USA

[2] Univ Utah, Hlth Sci Ctr, Dept Med, Salt Lake City, UT 84132 USA

[3] Univ Utah, Hlth Sci Ctr, Dept Biochem & Mitochondrial Proteome Partnership, Salt Lake City, UT 84132 USA

[4] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA

[5] Rutgers State Univ, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA

[6] Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08854 USA

[7] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA

[8] Univ Wisconsin, Dept Biochem & Mitochondrial Prot Partnership, Madison, WI 53562 USA

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 43期

基金：

美国国家卫生研究院;

关键词：

HUMAN-DISEASE GENES; PROTEIN; CONSERVATION; SEQUENCE; DATABASE;

D O I：

10.1021/bi301171u

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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.

引用

页码：8475 / 8477

页数：3

共 18 条

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].