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1mk1
From Proteopedia
(Difference between revisions)
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<StructureSection load='1mk1' size='340' side='right'caption='[[1mk1]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1mk1' size='340' side='right'caption='[[1mk1]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1mk1]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1mk1]] 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=1MK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MK1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk1 OCA], [https://pdbe.org/1mk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mk1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mk1 ProSAT]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O33199_MYCTO O33199_MYCTO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1mk1 ConSurf]. | </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=1mk1 ConSurf]. | ||
<div style="clear:both"></div> | <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 </= 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. | ||
| - | + | ==See Also== | |
| - | + | *[[ADP-ribose pyrophosphatase 3D structures|ADP-ribose pyrophosphatase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: ADP-ribose diphosphatase]] | ||
[[Category: Large Structures]] | [[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: Adenosine diphospho-ribose]] | ||
| - | [[Category: Adpr pyrophosphatase]] | ||
| - | [[Category: Adprase]] | ||
| - | [[Category: Hydrolase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
| - | [[Category: | + | [[Category: Amzel LM]] |
| - | [[Category: | + | [[Category: Bianchet MA]] |
| + | [[Category: Cunningham JE]] | ||
| + | [[Category: Gabelli SB]] | ||
| + | [[Category: Kang L-W]] | ||
| + | [[Category: O'Handley SF]] | ||
Current revision
Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme
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