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2h98
From Proteopedia
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| - | [[Image:2h98.gif|left|200px]]<br /><applet load="2h98" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2h98, resolution 1.800Å" /> | ||
| - | '''Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)'''<br /> | ||
| - | == | + | ==Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)== |
| - | + | <StructureSection load='2h98' size='340' side='right'caption='[[2h98]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2h98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi_ADP1 Acinetobacter baylyi ADP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H98 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]] 1.8Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2h98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h98 OCA], [https://pdbe.org/2h98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h98 RCSB], [https://www.ebi.ac.uk/pdbsum/2h98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h98 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/CATM_ACIAD CATM_ACIAD] Positively regulates the expression of catA, catBCIJFD and benPK in response to cis,cis-muconate. It binds to the catB-catM intercistronic region, to a specific sequence upstream of catA and to the benPK promoter region. Can also repress pca genes.<ref>PMID:7592340</ref> <ref>PMID:11932465</ref> <ref>PMID:12620848</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/h9/2h98_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=2h98 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acinetobacter baylyi ADP1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ezezika OC]] | ||
| + | [[Category: Momany C]] | ||
| + | [[Category: Neidle EL]] | ||
Current revision
Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)
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