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5j1j

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<StructureSection load='5j1j' size='340' side='right'caption='[[5j1j]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='5j1j' size='340' side='right'caption='[[5j1j]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5j1j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J1J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J1J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5j1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J1J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.55&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fleN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5j1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j1j OCA], [http://pdbe.org/5j1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j1j RCSB], [http://www.ebi.ac.uk/pdbsum/5j1j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j1j ProSAT]</span></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=5j1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j1j OCA], [https://pdbe.org/5j1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j1j RCSB], [https://www.ebi.ac.uk/pdbsum/5j1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j1j ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/FLEN_PSEAE FLEN_PSEAE] ATPase that plays an important role in maintaining flagellar number in Pseudomonas aeruginosa (PubMed:10629180, PubMed:28065505). Exhibits anti-activator activity against FleQ, the global transcriptional regulator of flagellar genes (PubMed:22581773, PubMed:28065505).<ref>PMID:10629180</ref> <ref>PMID:22581773</ref> <ref>PMID:28065505</ref>
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FleN, a P loop ATPase is vital for maintaining a monotrichous phenotype in Pseudomonas aeruginosa. FleN exhibits antagonistic activity against FleQ, the master transcriptional regulator of flagellar genes. Crystal structures of FleN in the apo form (1.66 A) and in complex with beta,gamma-imidoadenosine 5'-triphosphate (1.55 A) reveal that it undergoes drastic conformational changes on ATP binding to attain a structure capable of dimerization. Mutations of the residues that stabilize the binding of ATP were defective in their ability to dimerize and do not inhibit ATP hydrolysis by FleQ. Conversely, the catalytic mutant of FleN, was an efficient inhibitor. These observations posit that the dimer is the functional form of FleN and it is nucleotide binding and not hydrolysis by FleN that is necessary to exert an antagonistic effect against FleQ. Our study shows that ATP-induced dimerization may be a strategy to achieve reversible inhibition of FleQ to fine-tune the function of this activator to an optimal level.
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ATP-Induced Structural Remodeling in the Antiactivator FleN Enables Formation of the Functional Dimeric Form.,Chanchal, Banerjee P, Jain D Structure. 2017 Feb 7;25(2):243-252. doi: 10.1016/j.str.2016.11.022. Epub 2017, Jan 5. PMID:28065505<ref>PMID:28065505</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5j1j" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pseae]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Banerjee, P]]
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[[Category: Banerjee P]]
[[Category: Chanchal]]
[[Category: Chanchal]]
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[[Category: Jain, D]]
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[[Category: Jain D]]
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[[Category: Amppnp]]
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[[Category: Antiactivator]]
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[[Category: Flen]]
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[[Category: Transcription]]
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Current revision

Structure of FleN-AMPPNP complex

PDB ID 5j1j

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