2LM4
Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium Target YT682A
Summary for 2LM4
| Entry DOI | 10.2210/pdb2lm4/pdb |
| NMR Information | BMRB: 18098 |
| Descriptor | Succinate dehydrogenase assembly factor 2, mitochondrial (1 entity in total) |
| Functional Keywords | structural genomics, northeast structural genomics consortium (nesg), psi-biology, protein structure initiative, protein binding, mitochondrial protein partnership, mpp |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Mitochondrion matrix: Q08230 |
| Total number of polymer chains | 1 |
| Total formula weight | 13193.03 |
| Authors | 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) (deposition date: 2011-11-22, release date: 2012-01-04, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 23062074DOI: 10.1021/bi301171u PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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