1mqw
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Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme
OverviewOverview
Nudix hydrolases are a family of proteins that contain the characteristic, sequence GX(5)EX(7)REUXEEXG(I/L/V), the Nudix box. They catalyze the, hydrolysis of a variety of nucleoside diphosphate derivatives such as, ADP-ribose, Ap(n)A (3 </= n </= 6), NADH, and dATP. A number of Nudix, hydrolases from several species, ranging from bacteria to humans, have, been characterized, including, in some cases, the determination of their, three-dimensional structures. The product of the Rv1700 gene of M., tuberculosis is a Nudix hydrolase specific for ADP-ribose (ADPR). We have, determined the crystal structures of MT-ADPRase alone, and in complex with, substrate, with substrate and the nonactivating metal ion Gd(3+), and in, complex with a nonhydrolyzable ADPR analog and the activating metal ion, Mn(2+). These structures, refined with data extending to resolutions, between 2.0 and 2.3 A, showed that there are sequence differences in, binding site residues between MT-ADPRase and a human homolog that may be, exploited for antituberculosis drug development.
About this StructureAbout this Structure
1MQW is a Single protein structure of sequence from Mycobacterium tuberculosis with MN and ADV as ligands. Active as ADP-ribose diphosphatase, with EC number 3.6.1.13 Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis., Kang LW, Gabelli SB, Cunningham JE, O'Handley SF, Amzel LM, Structure. 2003 Aug;11(8):1015-23. PMID:12906832
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