4wxm

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==FleQ REC domain from Pseudomonas aeruginosa PAO1==
==FleQ REC domain from Pseudomonas aeruginosa PAO1==
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<StructureSection load='4wxm' size='340' side='right' caption='[[4wxm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4wxm' size='340' side='right'caption='[[4wxm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4wxm]] is a 5 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=4WXM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4wxm]] is a 5 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=4WXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXM FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wxo|4wxo]]</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]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fleQ, PA1097 ([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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxm OCA], [https://pdbe.org/4wxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxm RCSB], [https://www.ebi.ac.uk/pdbsum/4wxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxm ProSAT]</span></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=4wxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxm OCA], [http://pdbe.org/4wxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxm RCSB], [http://www.ebi.ac.uk/pdbsum/4wxm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxm ProSAT]</span></td></tr>
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</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/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>
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FleQ is an AAA+ ATPase enhancer-binding protein that regulates both flagella and biofilm formation in the opportunistic pathogen Pseudomonas aeruginosa. FleQ belongs to the NtrC subfamily of response regulators, but lacks the corresponding aspartic acid for phosphorylation in the REC domain (FleQ(R), also named FleQ domain). Here, we show that the atypical REC domain of FleQ is essential for the function of FleQ. Crystal structure of FleQ(R) at 2.3A reveals that the structure of FleQ(R) is significantly different from the REC domain of NtrC1 which regulates gene expression in a phosphorylation dependent manner. FleQ(R) forms a novel active dimer (transverse dimer), and mediates the dimerization of full-length FleQ in an unusual manner. Point mutations that affect the dimerization of FleQ lead to loss of function of the protein. Moreover, a c-di-GMP binding site deviating from the previous reported one is identified through structure analysis and point mutations.
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The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator.,Su T, Liu S, Wang K, Chi K, Zhu D, Wei T, Huang Y, Guo L, Hu W, Xu S, Lin Z, Gu L J Struct Biol. 2015 Oct;192(1):1-13. doi: 10.1016/j.jsb.2015.09.002. Epub 2015, Sep 8. PMID:26362077<ref>PMID:26362077</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 4wxm" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pseae]]
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[[Category: Large Structures]]
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[[Category: Gu, L]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Liu, S]]
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[[Category: Gu L]]
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[[Category: Su, T]]
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[[Category: Liu S]]
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[[Category: Biofilm]]
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[[Category: Su T]]
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[[Category: C-di-gmp binding]]
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[[Category: Ntrc superfamily]]
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[[Category: Regulatory domain]]
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[[Category: Transcription regulator]]
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Current revision

FleQ REC domain from Pseudomonas aeruginosa PAO1

PDB ID 4wxm

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