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New page: left|200px<br /><applet load="1mp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mp2, resolution 2.3Å" /> '''Structure of MT-ADPRa...
 
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[[Image:1mp2.jpg|left|200px]]<br /><applet load="1mp2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mp2, resolution 2.3&Aring;" />
'''Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis'''<br />


==Overview==
==Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis==
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.
<StructureSection load='1mp2' size='340' side='right'caption='[[1mp2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mp2]] 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=1MP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MP2 FirstGlance]. <br>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp2 OCA], [https://pdbe.org/1mp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mp2 RCSB], [https://www.ebi.ac.uk/pdbsum/1mp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mp2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O33199_MYCTO O33199_MYCTO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/1mp2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mp2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MP2 OCA].
*[[ADP-ribose pyrophosphatase 3D structures|ADP-ribose pyrophosphatase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Large Structures]]
[[Category: ADP-ribose diphosphatase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Amzel LM]]
[[Category: Amzel, L.M.]]
[[Category: Bianchet MA]]
[[Category: Bianchet, M.A.]]
[[Category: Cunningham JE]]
[[Category: Cunningham, J.E.]]
[[Category: Gabelli SB]]
[[Category: Gabelli, S.B.]]
[[Category: Kang L-W]]
[[Category: Handley, S.F.O.]]
[[Category: O'Handley SF]]
[[Category: Kang, L.W.]]
[[Category: adpr]]
[[Category: adprase]]
[[Category: mycobacterium tuberculosis]]
[[Category: nudix hydrolase]]
[[Category: rv1700]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:45:58 2007''

Latest revision as of 07:46, 14 February 2024

Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis

1mp2, resolution 2.30Å

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