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4rnh

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<StructureSection load='4rnh' size='340' side='right'caption='[[4rnh]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='4rnh' size='340' side='right'caption='[[4rnh]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rnh]] is a 1 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=4RNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RNH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rnh]] is a 1 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=4RNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RNH 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=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rnf|4rnf]], [[4rni|4rni]], [[4rnj|4rnj]]</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=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">morA, PA4601 ([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=4rnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnh OCA], [https://pdbe.org/4rnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rnh RCSB], [https://www.ebi.ac.uk/pdbsum/4rnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rnh 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=4rnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnh OCA], [http://pdbe.org/4rnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rnh RCSB], [http://www.ebi.ac.uk/pdbsum/4rnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rnh 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/Q9HVI8_PSEAE Q9HVI8_PSEAE]
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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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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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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 4rnh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</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: Phippen, C W]]
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[[Category: Phippen CW]]
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[[Category: Tews, I]]
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[[Category: Tews I]]
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[[Category: C-di-gmp]]
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[[Category: Diguanylate cyclase]]
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[[Category: Gtp]]
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[[Category: Hydrolase]]
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[[Category: Phosphodiesterase]]
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[[Category: Tandem ggdef and eal domain]]
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[[Category: Transferase]]
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Current revision

PaMorA tandem diguanylate cyclase - phosphodiesterase, c-di-GMP complex

PDB ID 4rnh

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