6jdl

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'''Unreleased structure'''
 
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The entry 6jdl is ON HOLD until Paper Publication
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==Central domain of FleQ H287A mutant in complex with ATPgS and Mg==
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<StructureSection load='6jdl' size='340' side='right'caption='[[6jdl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6jdl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JDL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JDL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jdl OCA], [http://pdbe.org/6jdl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jdl RCSB], [http://www.ebi.ac.uk/pdbsum/6jdl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jdl ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Jain, D., Banerjee, P., Chanchal
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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>
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Description: Central domain of FleQ H287A mutant in complex with ATPgS and Mg
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Chanchal]]
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<div class="pdbe-citations 6jdl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Banerjee, P]]
[[Category: Banerjee, P]]
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[[Category: Chanchal]]
[[Category: Jain, D]]
[[Category: Jain, D]]
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[[Category: Aaa+]]
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[[Category: Fleq]]
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[[Category: Ntrc]]
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[[Category: Pseudomona]]
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[[Category: Transcription]]

Revision as of 06:46, 27 November 2019

Central domain of FleQ H287A mutant in complex with ATPgS and Mg

PDB ID 6jdl

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