1x74
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1x74.png|left|200px]] | ||
- | + | ==Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site== | |
- | + | <StructureSection load='1x74' size='340' side='right'caption='[[1x74]], [[Resolution|resolution]] 1.79Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1x74]] is a 4 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=1X74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X74 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]] 1.79Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1x74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x74 OCA], [https://pdbe.org/1x74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x74 RCSB], [https://www.ebi.ac.uk/pdbsum/1x74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x74 ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/AMACR_MYCTU AMACR_MYCTU] Catalyzes the epimerization of (2R)- and (2S)-methylacyl-coenzyme A (CoA) thioesters (PubMed:15632186, PubMed:19854148, PubMed:26348625). Accepts as substrates a wide range of alpha-methylacyl-CoAs, including (2R)-2-methylmyristoyl-CoA and (2S)-2-methylmyristoyl-CoA, (2R)-pristanoyl-CoA and (2S)-pristanoyl-CoA, and the cholesterol esters (25R)-3-oxo-cholest-4-en-26-oyl-CoA and (25S)-3-oxo-cholest-4-en-26-oyl-CoA (PubMed:15632186, PubMed:26348625). Can also catalyze the interconversion of the non-physiologic substrates (2R)-ibuprofenoyl-CoA and (2S)-ibuprofenoyl-CoA, which are potential competitive inhibitors of the enzyme (PubMed:19854148).<ref>PMID:15632186</ref> <ref>PMID:19854148</ref> <ref>PMID:26348625</ref> | |
- | + | == 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/x7/1x74_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=1x74 ConSurf]. | |
- | + | <div style="clear:both"></div> | |
- | == | + | == References == |
- | + | <references/> | |
- | [[Category: | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
- | + | [[Category: Bhaumik P]] | |
- | [[Category: Bhaumik | + | [[Category: Conzelmann E]] |
- | [[Category: Conzelmann | + | [[Category: Hiltunen JK]] |
- | [[Category: Hiltunen | + | [[Category: Kalle S]] |
- | [[Category: Kalle | + | [[Category: Kotti TJ]] |
- | [[Category: Kotti | + | [[Category: Schmitz W]] |
- | [[Category: Schmitz | + | [[Category: Wierenga RK]] |
- | [[Category: Wierenga | + | |
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Current revision
Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site
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