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Journal of Bacteriology, December 2004, p. 8083-8088, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8083-8088.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Guennadi Kozlov,1 Demetra Elias,1 Anthony Semesi,2 Adelinda Yee,2 Miroslaw Cygler,3 and Kalle Gehring1*

Department of Biochemistry, McGill University,1 Macromolecular Structure Group, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec,3 Clinical Genomics Center: Proteomics, University Health Network, Toronto, Ontario, Canada2

Received 19 May 2004/ Accepted 19 August 2004

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 ß{alpha}ßß{alpha}ß fold with two {alpha}-helices on one side of a four-strand antiparallel ß-sheet. The ß2-ß3 loop shows the highest sequence conservation and is likely functionally important. The ß-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.

* Corresponding author. Mailing address: Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6. Phone: (514) 398-7287. Fax: (514) 398-7384. E-mail: kalle.gehring{at}mcgill.ca.

Journal of Bacteriology, December 2004, p. 8083-8088, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8083-8088.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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  • Grant, G. A. (2006). The ACT Domain: A Small Molecule Binding Domain and Its Role as a Common Regulatory Element. J. Biol. Chem. 281: 33825-33829 [Full Text]  


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