1mqe: Difference between revisions
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[[Image:1mqe.jpg|left|200px]] | [[Image:1mqe.jpg|left|200px]] | ||
'''Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, a Nudix enzyme''' | {{Structure | ||
|PDB= 1mqe |SIZE=350|CAPTION= <scene name='initialview01'>1mqe</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene> and <scene name='pdbligand=GD3:GADOLINIUM ION'>GD3</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] | |||
|GENE= | |||
}} | |||
'''Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, a Nudix enzyme''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MQE is a [ | 1MQE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQE OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12906832 12906832] | ||
[[Category: ADP-ribose diphosphatase]] | [[Category: ADP-ribose diphosphatase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: rv1700]] | [[Category: rv1700]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:49 2008'' | ||
Revision as of 13:46, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | ADP-ribose diphosphatase, with EC number 3.6.1.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, 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
1MQE 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
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