1ojl
From Proteopedia
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| - | [[Image:1ojl.gif|left|200px]] | ||
| - | < | + | ==Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding== |
| - | + | <StructureSection load='1ojl' size='340' side='right'caption='[[1ojl]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1ojl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJL 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]] 3Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=1ojl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojl OCA], [https://pdbe.org/1ojl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ojl RCSB], [https://www.ebi.ac.uk/pdbsum/1ojl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojl ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/ZRAR_SALTY ZRAR_SALTY] Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity). | |
| - | + | == 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/oj/1ojl_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=1ojl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The sigma(54)-dependent transcription in bacteria is associated with various stress and growth conditions. Activators of the sigma(54) protein contain a central domain belonging to the AAA+ superfamily of ATPases, members of which function in diverse cellular processes in both prokaryotic and eukaryotic cells. We describe the X-ray structure of an N-terminal domain deletion of the ZraR protein from Salmonella typhimurium, which is a homologue of the general nitrogen regulatory protein NtrC, at 3A resolution. The structure reveals a hexameric ring that is typical for AAA+ containing proteins but which differs from the heptameric ring found in the crystal structure of the AAA+ domain of NtrC1 from Aquifex aeolicus. The dimerisation interface between DNA-binding domains observed in the crystal structure suggests that dodecamers, rather than hexamers, might be the functionally important oligomer. | The sigma(54)-dependent transcription in bacteria is associated with various stress and growth conditions. Activators of the sigma(54) protein contain a central domain belonging to the AAA+ superfamily of ATPases, members of which function in diverse cellular processes in both prokaryotic and eukaryotic cells. We describe the X-ray structure of an N-terminal domain deletion of the ZraR protein from Salmonella typhimurium, which is a homologue of the general nitrogen regulatory protein NtrC, at 3A resolution. The structure reveals a hexameric ring that is typical for AAA+ containing proteins but which differs from the heptameric ring found in the crystal structure of the AAA+ domain of NtrC1 from Aquifex aeolicus. The dimerisation interface between DNA-binding domains observed in the crystal structure suggests that dodecamers, rather than hexamers, might be the functionally important oligomer. | ||
| - | + | Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR.,Sallai L, Tucker PA J Struct Biol. 2005 Aug;151(2):160-70. PMID:16005641<ref>PMID:16005641</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1ojl" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Sallai | + | <references/> |
| - | [[Category: Tucker | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | |
| - | + | [[Category: Sallai L]] | |
| - | + | [[Category: Tucker PA]] | |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding
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