1mqw: Difference between revisions
New page: left|200px<br /><applet load="1mqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqw, resolution 2.3Å" /> '''Structure of the MT-A... |
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[[Image:1mqw.jpg|left|200px]]<br /><applet load="1mqw" size=" | [[Image:1mqw.jpg|left|200px]]<br /><applet load="1mqw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1mqw, resolution 2.3Å" /> | caption="1mqw, resolution 2.3Å" /> | ||
'''Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme'''<br /> | '''Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme'''<br /> | ||
==Overview== | ==Overview== | ||
Nudix hydrolases are a family of proteins that contain the characteristic | 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 Structure== | ==About this Structure== | ||
1MQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MN and ADV as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1MQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ADV:'>ADV</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Amzel, L | [[Category: Amzel, L M.]] | ||
[[Category: Bianchet, M | [[Category: Bianchet, M A.]] | ||
[[Category: Cunningham, J | [[Category: Cunningham, J E.]] | ||
[[Category: Gabelli, S | [[Category: Gabelli, S B.]] | ||
[[Category: Handley, S | [[Category: Handley, S F.O.]] | ||
[[Category: Kang, L | [[Category: Kang, L W.]] | ||
[[Category: ADV]] | [[Category: ADV]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: rv1700]] | [[Category: rv1700]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:06 2008'' | ||
Revision as of 14:58, 21 February 2008
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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 and 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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