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Papers In Press, published online ahead of print January 2, 2003
Biochemistry & Biophysics, Texas A&M University, College Station, TX 77843-2128
Corresponding Author: yoonsang{at}tamu.edu
The N-1-(5'-phosphoribosyl)-ATP transferase (ATP-PRTase) 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 ATP-PRTase 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 while the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of 3 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.
J. Biol. Chem, 10.1074/jbc.M212124200
Submitted on November 27, 2002
Revised on December 26, 2002
Accepted on January 2, 2003
Crystal structure of ATP Phosphoribosyltransferase from Mycobacterium tuberculosis
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