View source for 6jdi


==Central domain of FleQ H287N mutant in complex with ATPgS and Mg==
<StructureSection load='6jdi' size='340' side='right'caption='[[6jdi]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JDI 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6jdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jdi OCA], [https://pdbe.org/6jdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jdi RCSB], [https://www.ebi.ac.uk/pdbsum/6jdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jdi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLEQ_PSEAE FLEQ_PSEAE] AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:9287015, PubMed:11673434, PubMed:26362077). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773).<ref>PMID:11673434</ref> <ref>PMID:22581773</ref> <ref>PMID:26362077</ref> <ref>PMID:9287015</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of the AAA+ (ATPase associated with various cellular activities) family of ATPases couple chemical energy derived from ATP hydrolysis for generation of mechanical force, resulting in conformational changes. The hydrolysis is brought about by highly conserved domains and motifs. The sensor I motif is critical for sensing and hydrolysis of the nucleotide. Pseudomonas aeruginosa FleQ is an ATPase that is a positive regulator of flagellar gene expression. We have determined the crystal structures of the ATPase domain of wild-type FleQ and sensor I mutants H287N and H287A in complex with ATPgammaS and Mg(2+) to 2.4, 1.95, and 2.25 A resolution, respectively. The structural data highlight the role of sensor I in regulating the ATPase activity. The in vitro and in vivo data demonstrate that the moderate ATPase activity of FleQ due to the presence of histidine in sensor I is essential for maintaining the monotrichous phenotype and for the rapid motility to biofilm transition.

Sensor I Regulated ATPase Activity of FleQ Is Essential for Motility to Biofilm Transition in Pseudomonas aeruginosa.,Banerjee P, Chanchal, Jain D ACS Chem Biol. 2019 Jul 19;14(7):1515-1527. doi: 10.1021/acschembio.9b00255. Epub, 2019 Jul 3. PMID:31268665<ref>PMID:31268665</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jdi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Banerjee P]]
[[Category: Chanchal]]
[[Category: Jain D]]