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Structural Similarity of YbeD Protein from Escherichia coli to Allosteric Regulatory Domains

2004; American Society for Microbiology; Volume: 186; Issue: 23 Linguagem: Inglês

10.1128/jb.186.23.8083-8088.2004

1098-5530

Guennadi Kozlov, Demetra Elias, Anthony Semesi, Adelinda Yee, Mirosław Cygler, Kalle Gehring,

Metabolism and Genetic Disorders

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 βαββαβ fold with two α-helices on one side of a four-strand antiparallel β-sheet. The β2-β3 loop shows the highest sequence conservation and is likely functionally important. The β-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.