2LM4: Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium Target YT682A

Citation:
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.
PDB ID: 2LM4Download
MMDB ID: 96202
PDB Deposition Date: 2011/11/22
Updated in MMDB: 2012/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LM4: monomeric; determined by author
Molecular Components in 2LM4
Label Count Molecule
Protein (1 molecule)
1
Succinate Dehydrogenase Assembly Factor 2, Mitochondrial(Gene symbol: SDH5)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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