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J. Biol. Chem., Vol. 279, Issue 4, 2704-2711, January 23, 2004

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Three-dimensional Structure of YaaE from Bacillus subtilis, a Glutaminase Implicated in Pyridoxal-5'-phosphate Biosynthesis^*

Jacob A. Bauer, Eric M. Bennett, Tadhg P. Begley, and Steven E. Ealick

From the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853

The structure of YaaE from Bacillus subtilis was determined at 2.5-Å resolution. YaaE is a member of the triad glutamine aminotransferase family and functions in a recently identified alternate pathway for the biosynthesis of vitamin B₆. Proposed active residues include conserved Cys-79, His-170, and Glu-172. YaaE shows similarity to HisH, a glutaminase involved in histidine biosynthesis. YaaD associates with YaaE. A homology model of this protein was constructed. YaaD is predicted to be a (/)₈ barrel on the basis of sequence comparisons. The predicted active site includes highly conserved residues 211–216 and 233–235. Finally, a homology model of a putative YaaD-YaaE complex was prepared using the structure of HisH-F as a model. This model predicts that the ammonia molecule generated by YaaE is channeled through the center of the YaaD barrel to the putative YaaD active site.

Received for publication, September 17, 2003 , and in revised form, October 27, 2003.

^* This research was sponsored in part by National Institutes of Health Grants RR-15301 and DK44083. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 1R9G) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence should be addressed. Tel.: 607-255-7961; Fax: 607-255-1227; E-mail: see3{at}cornell.edu.

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