1mp2: Difference between revisions

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 <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 [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1MP2 FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mk1|1mk1]], [[1mqe|1mqe]], [[1mqw|1mqw]], [[1mr2|1mr2]]</div></td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RV1700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp2 OCA], [http://pdbe.org/1mp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mp2 RCSB], [http://www.ebi.ac.uk/pdbsum/1mp2 PDBsum], [http://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]]
@@ Line 19: / Line 19: @@
 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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<ref>PMID:12906832</ref>
+==See Also==
+*[[ADP-ribose pyrophosphatase 3D structures|ADP-ribose pyrophosphatase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mp2" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: ADP-ribose diphosphatase]]
 [[Category: Large Structures]]
-[[Category: Amzel, L M]]
-[[Category: Bianchet, M A]]
-[[Category: Cunningham, J E]]
-[[Category: Gabelli, S B]]
-[[Category: Handley, S F.O]]
-[[Category: Kang, L W]]
-[[Category: Adpr]]
-[[Category: Adprase]]
-[[Category: Hydrolase]]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Nudix hydrolase]]
+[[Category: Amzel LM]]
-[[Category: Rv1700]]
+[[Category: Bianchet MA]]
+[[Category: Cunningham JE]]
+[[Category: Gabelli SB]]
+[[Category: Kang L-W]]
+[[Category: O'Handley SF]]