1mqw

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[[Image:1mqw.jpg|left|200px]]<br /><applet load="1mqw" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mqw, resolution 2.3&Aring;" />
 
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'''Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme'''<br />
 
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==Overview==
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==Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme==
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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 &lt;/= n &lt;/= 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.
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<StructureSection load='1mqw' size='340' side='right'caption='[[1mqw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADV:ALPHA-BETA+METHYLENE+ADP-RIBOSE'>ADV</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqw OCA], [https://pdbe.org/1mqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqw RCSB], [https://www.ebi.ac.uk/pdbsum/1mqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O33199_MYCTO O33199_MYCTO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mq/1mqw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mqw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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].
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*[[ADP-ribose pyrophosphatase 3D structures|ADP-ribose pyrophosphatase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12906832 12906832]
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[[Category: Large Structures]]
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[[Category: ADP-ribose diphosphatase]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Amzel LM]]
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[[Category: Amzel, L M.]]
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[[Category: Bianchet MA]]
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[[Category: Bianchet, M A.]]
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[[Category: Cunningham JE]]
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[[Category: Cunningham, J E.]]
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[[Category: Gabelli SB]]
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[[Category: Gabelli, S B.]]
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[[Category: Kang L-W]]
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[[Category: Handley, S F.O.]]
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[[Category: O'Handley SF]]
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[[Category: Kang, L W.]]
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[[Category: ADV]]
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[[Category: MN]]
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[[Category: adpr]]
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[[Category: mycobacterium tuberculosis]]
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[[Category: nudix hydrolase]]
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[[Category: rv1700]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:06 2008''
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Current revision

Structure of the MT-ADPRase in complex with three Mn2+ ions and AMPCPR, a Nudix enzyme

PDB ID 1mqw

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