6kkp

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'''Unreleased structure'''
 
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The entry 6kkp is ON HOLD until Paper Publication
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==The crystal structure of apo-SiaC from Pseudomonas aeruginosa==
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<StructureSection load='6kkp' size='340' side='right'caption='[[6kkp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6kkp]] 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=6KKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KKP FirstGlance]. <br>
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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]] 2.5&#8491;</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=6kkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kkp OCA], [https://pdbe.org/6kkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kkp RCSB], [https://www.ebi.ac.uk/pdbsum/6kkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kkp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9I6W2_PSEAE Q9I6W2_PSEAE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial cyclic-di-GMP (c-di-GMP) production is associated with biofilm development and the switch from acute to chronic infections. In Pseudomonas aeruginosa, the diguanylate cyclase (DGC) SiaD and phosphatase SiaA, which are co-transcribed as part of a siaABCD operon, are essential for cellular aggregation. However, the detailed functions of this operon and the relationships among its constituent genes are unknown. Here, we demonstrate that the siaABCD operon encodes for a signaling network that regulates SiaD enzymatic activity to control biofilm and aggregates formation. Through protein-protein interaction, SiaC promotes SiaD diguanylate cyclase activity. Biochemical and structural data revealed that SiaB is an unusual protein kinase that phosphorylates SiaC, whereas SiaA phosphatase can dephosphorylate SiaC. The phosphorylation state of SiaC is critical for its interaction with SiaD, which will switch on or off the DGC activity of SiaD and regulate c-di-GMP levels and subsequent virulence phenotypes. Collectively, our data provide insights into the molecular mechanisms underlying the modulation of DGC activity associated with chronic infections, which may facilitate the development of antimicrobial drugs.
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Authors:
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The SiaA/B/C/D signaling network regulates biofilm formation in Pseudomonas aeruginosa.,Chen G, Gan J, Yang C, Zuo Y, Peng J, Li M, Huo W, Xie Y, Zhang Y, Wang T, Deng X, Liang H EMBO J. 2020 Mar 16;39(6):e103412. doi: 10.15252/embj.2019103412. Epub 2020 Feb, 24. PMID:32090355<ref>PMID:32090355</ref>
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Description:
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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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<div class="pdbe-citations 6kkp" 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]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Chen GK]]
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[[Category: Gan JH]]
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[[Category: Liang HH]]
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[[Category: Yang C]]

Current revision

The crystal structure of apo-SiaC from Pseudomonas aeruginosa

PDB ID 6kkp

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