2h98
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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)== | ||
| - | <StructureSection load='2h98' size='340' side='right' caption='[[2h98]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='2h98' size='340' side='right'caption='[[2h98]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2h98]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2h98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aciad Aciad]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </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='related'><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> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f7b|2f7b]], [[2f7c|2f7c]], [[2f7a|2f7a]], [[2f78|2f78]], [[2h99|2h99]], [[2h9b|2h9b]], [[2h9q|2h9q]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">catM, catR ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">catM, catR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=62977 ACIAD])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/2h98_consurf.spt"</scriptWhenChecked> | + | <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> | ||
| Line 21: | Line 21: | ||
</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]. | </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> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 29: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aciad]] | [[Category: Aciad]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ezezika, O C]] | [[Category: Ezezika, O C]] | ||
[[Category: Momany, C]] | [[Category: Momany, C]] | ||
Revision as of 07:34, 17 March 2021
Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)
| |||||||||||
Categories: Aciad | Large Structures | Ezezika, O C | Momany, C | Neidle, E L | Acinetobacter | Benm | Catm | Lttr | Transcription | Transcriptional regulator
