Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis

被引：76
作者：
Cho, Y
Sharma, V
Sacchettini, JC [1 ]
机构：
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[2] Texas A&M Univ, Syst Hlth Sci Ctr, Grad Sch Biomed Sci, College Stn, TX 77843 USA
[3] Inst Biosci & Technol, Ctr Struct Biol, Houston, TX 77030 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2003年 / 278卷 / 10期
关键词：
D O I：
10.1074/jbc.M212124200
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 Angstrom resolution and without ligands to 2.7 Angstrom 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.
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页码：8333 / 8339
页数：7
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