Download MendeleyStructural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains
Kozlov, G., Elias, D., Semesi, A., Yee, A., Cygler, M., Gehring, K.(2004) J Bacteriol 186: 8083-8088
- PubMed: 15547281
- DOI: https://doi.org/10.1128/JB.186.23.8083-8088.2004
- Primary Citation of Related Structures:
1RWU - PubMed 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.
Organizational Affiliation:
Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G 1Y6.
