PMID:15547281

Citation	Kozlov, G, Elias, D, Semesi, A, Yee, A, Cygler, M and Gehring, K (2004) Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains. J. Bacteriol. 186:8083-8
Abstract	Lipoic acid is an essential prosthetic group in several metabolic pathways. The biosynthetic pathway of protein lipoylation in Escherichia coli involves gene products of the lip operon. YbeD is a conserved bacterial protein located in the dacA-lipB intergenic region. Here, we report the nuclear magnetic resonance structure of YbeD from E. coli. The structure includes a beta alpha beta beta alpha beta fold with two alpha-helices on one side of a four-strand antiparallel beta-sheet. The beta 2-beta 3 loop shows the highest sequence conservation and is likely functionally important. The beta-sheet surface contains a patch of conserved hydrophobic residues, suggesting a role in protein-protein interactions. YbeD shows striking structural homology to the regulatory domain from d-3-phosphoglycerate dehydrogenase, hinting at a role in the allosteric regulation of lipoic acid biosynthesis or the glycine cleavage system.
Links	PubMed PMC529071 Online version:10.1128/JB.186.23.8083-8088.2004
Keywords	Allosteric Regulation; Amino Acid Sequence; Escherichia coli Proteins/chemistry; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Serine-Type D-Ala-D-Ala Carboxypeptidase/chemistry; Thioctic Acid/biosynthesis
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