This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Teplyakov, A. Articles by Gilliland, G. L. Search for Related Content PubMed PubMed Citation Articles by Teplyakov, A. Articles by Gilliland, G. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2004, p. 7134-7140, Vol. 186, No. 21
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.21.7134-7140.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the YgfZ Protein from Escherichia coli Suggests a Folate-Dependent Regulatory Role in One-Carbon Metabolism

Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, and National Institute of Standards and Technology, Rockville, Maryland,¹ Center for Synchrotron Radiation Research and Instrumentation, Biological, Chemical and Physical Sciences Department, Illinois Institute of Technology, Chicago, Illinois²

Received 6 May 2004/ Accepted 9 August 2004

The ygfZ gene product of Escherichia coli represents a large protein family conserved in bacteria to eukaryotes. The members of this family are uncharacterized proteins with marginal sequence similarity to the T-protein (aminomethyltransferase) of the glycine cleavage system. To assist with the functional assignment of the YgfZ family, the crystal structure of the E. coli protein was determined by multiwavelength anomalous diffraction. The protein molecule has a three-domain architecture with a central hydrophobic channel. The structure is very similar to that of bacterial dimethylglycine oxidase, an enzyme of the glycine betaine pathway and a homolog of the T-protein. Based on structural superposition, a folate-binding site was identified in the central channel of YgfZ, and the ability of YgfZ to bind folate derivatives was confirmed experimentally. However, in contrast to dimethylglycine oxidase and T-protein, the YgfZ family lacks amino acid conservation at the folate site, which implies that YgfZ is not an aminomethyltransferase but is likely a folate-dependent regulatory protein involved in one-carbon metabolism.

This article has been cited by other articles:

• Chen, J.-W., Sun, C.-M., Sheng, W.-L., Wang, Y.-C., Syu, W.-J. (2006). Expression Analysis of Up-Regulated Genes Responding to Plumbagin in Escherichia coli. J. Bacteriol. 188: 456-463 [Abstract] [Full Text]