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J. Biol. Chem., Vol. 278, Issue 10, 8333-8339, March 7, 2003

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Crystal Structure of ATP Phosphoribosyltransferase from Mycobacterium tuberculosis^*

Yoonsang Cho^§, Vivek Sharma^¶, and James C. Sacchettini^¶

From the  Department of Biochemistry and Biophysics, Texas A & M University, College Station, Texas 77843-2128, ^§ Graduate School of Biomedical Sciences, Texas A & M University System Health Science Center, College Station, Texas 77843-1114, and ^¶ Center for Structural Biology, Institute of Biosciences and Technology, Houston, Texas 77030-3303

The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 Å resolution and without ligands to 2.7 Å resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures.

The atomic coordinates and structure factors (codes 1NH7 and 1NH8 ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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