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J. Biol. Chem., Vol. 280, Issue 30, 27914-27923, July 29, 2005

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A New Arrangement of (/)₈ Barrels in the Synthase Subunit of PLP Synthase^*

Jianghai Zhu, John W. Burgner, Etti Harms, Boris R. Belitsky¶, and Janet L. Smith||

From the Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, the Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, and the ^¶Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Pyridoxal 5'-phosphate (PLP, vitamin B₆), a cofactor in many enzymatic reactions, has two distinct biosynthetic routes, which do not coexist in any organism. Two proteins, known as PdxS and PdxT, together form a PLP synthase in plants, fungi, archaea, and some eubacteria. PLP synthase is a heteromeric glutamine amidotransferase in which PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. In the 2.2-Å crystal structure, PdxS is a cylindrical dodecamer of subunits having the classic (/)₈ barrel fold. PdxS subunits form two hexameric rings with the active sites positioned on the inside. The hexamer and dodecamer forms coexist in solution. A novel phosphate-binding site is suggested by bound sulfate. The sulfate and another bound molecule, methyl pentanediol, were used to model the substrate ribulose 5-phosphate, and to propose catalytic roles for residues in the active site. The distribution of conserved surfaces in the PdxS dodecamer was used to predict a docking site for the glutaminase partner, PdxT.

Received for publication, April 4, 2005 , and in revised form, May 12, 2005.

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

^* This work was supported by National Institutes of Health Grant DK42303 (to J. L. S.) and National Science Foundation Grant MCB-0110651 (to B. R. B.). 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.

This article was selected as a Paper of the Week.

^|| To whom correspondence should be addressed: Life Sciences Inst., University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109. Tel.: 734-615-9564; Fax: 734-764-9492; E-mail: JanetSmith{at}umich.edu.

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