1MQW: Structure Of The Mt-adprase In Complex With Three Mn2+ Ions And Ampcpr, A Nudix Enzyme

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.
PDB ID: 1MQWDownload
MMDB ID: 24213
PDB Deposition Date: 2002/9/17
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1MQW: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1MQW
Label Count Molecule
Proteins (2 molecules)
Adpr Pyrophosphatase
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

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