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2h98

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==Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)==
==Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)==
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<StructureSection load='2h98' size='340' side='right' caption='[[2h98]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='2h98' size='340' side='right'caption='[[2h98]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2h98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_sp._adp1 Acinetobacter sp. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H98 FirstGlance]. <br>
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f7b|2f7b]], [[2f7c|2f7c]], [[2f7a|2f7a]], [[2f78|2f78]], [[2h99|2h99]], [[2h9b|2h9b]], [[2h9q|2h9q]]</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">catM, catR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=62977 Acinetobacter sp. ADP1])</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h98 RCSB], [http://www.ebi.ac.uk/pdbsum/2h98 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/2h98_consurf.spt"</scriptWhenChecked>
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<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>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2h98 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acinetobacter sp. adp1]]
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[[Category: Acinetobacter baylyi ADP1]]
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[[Category: Ezezika, O C.]]
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[[Category: Large Structures]]
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[[Category: Momany, C.]]
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[[Category: Ezezika OC]]
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[[Category: Neidle, E L.]]
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[[Category: Momany C]]
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[[Category: Acinetobacter]]
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[[Category: Neidle EL]]
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[[Category: Benm]]
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[[Category: Catm]]
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[[Category: Lttr]]
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[[Category: Transcription]]
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[[Category: Transcriptional regulator]]
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Current revision

Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)

PDB ID 2h98

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