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4rnj

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'''Unreleased structure'''
 
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The entry 4rnj is ON HOLD
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==PaMorA phosphodiesterase domain, apo form==
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<StructureSection load='4rnj' size='340' side='right'caption='[[4rnj]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4rnj]] 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=4RNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RNJ 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]] 2.32&#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=4rnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnj OCA], [https://pdbe.org/4rnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rnj RCSB], [https://www.ebi.ac.uk/pdbsum/4rnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rnj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9HVI8_PSEAE Q9HVI8_PSEAE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Diguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively synthesise and hydrolyse the secondary messenger cyclic dimeric GMP (c-di-GMP), and both activities are often found in a single protein. Intracellular c-di-GMP levels in turn regulate bacterial motility, virulence and biofilm formation. We report the first structure of a tandem DGC-PDE fragment, in which the catalytic domains are shown to be active. Two phosphodiesterase states are distinguished by active site formation. The structures, in the presence or absence of c-di-GMP, suggest that dimerisation and binding pocket formation are linked, with dimerisation being required for catalytic activity. An understanding of PDE activation is important, as biofilm dispersal via c-di-GMP hydrolysis has therapeutic effects on chronic infections.
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Authors: Phippen, C.W., Tews, I.
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Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator.,Phippen CW, Mikolajek H, Schlaefli HG, Keevil CW, Webb JS, Tews I FEBS Lett. 2014 Dec 20;588(24):4631-6. doi: 10.1016/j.febslet.2014.11.002. Epub, 2014 Nov 11. PMID:25447517<ref>PMID:25447517</ref>
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Description: PaMorA phosphodiesterase domain, apo form
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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 4rnj" 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 PAO1]]
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[[Category: Phippen CW]]
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[[Category: Tews I]]

Current revision

PaMorA phosphodiesterase domain, apo form

PDB ID 4rnj

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