1mqw
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | Rv1700 (Mycobacterium tuberculosis) | ||||||
| Activity: | ADP-ribose diphosphatase, with EC number 3.6.1.13 | ||||||
| Related: | 1mk1, 1mp2, 1MQW, 1MR2
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:19:56 2008