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| {{STRUCTURE_1mqw| PDB=1mqw | SCENE= }} | | {{STRUCTURE_1mqw| PDB=1mqw | SCENE= }} |
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| '''Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme'''
| | ===Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12906832}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12906832 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12906832}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nudix hydrolase]] | | [[Category: Nudix hydrolase]] |
| [[Category: Rv1700]] | | [[Category: Rv1700]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:36:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:24:23 2008'' |