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| | <StructureSection load='4rni' size='340' side='right'caption='[[4rni]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='4rni' size='340' side='right'caption='[[4rni]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rni]] 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=4RNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RNI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rni]] 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=4RNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RNI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rnf|4rnf]], [[4rnh|4rnh]], [[4rnj|4rnj]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rni OCA], [https://pdbe.org/4rni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rni RCSB], [https://www.ebi.ac.uk/pdbsum/4rni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rni ProSAT]</span></td></tr> |
| - | <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>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclic-guanylate-specific_phosphodiesterase Cyclic-guanylate-specific phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.52 3.1.4.52] </span></td></tr>
| + | |
| - | <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=4rni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rni OCA], [http://pdbe.org/4rni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rni RCSB], [http://www.ebi.ac.uk/pdbsum/4rni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rni ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9HVI8_PSEAE Q9HVI8_PSEAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cyclic-guanylate-specific phosphodiesterase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Phippen, C W]] | + | [[Category: Phippen CW]] |
| - | [[Category: Tews, I]] | + | [[Category: Tews I]] |
| - | [[Category: C-di-gmp]]
| + | |
| - | [[Category: Eal domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phosphodiesterase]]
| + | |
| Structural highlights
Function
Q9HVI8_PSEAE
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Phippen CW, Mikolajek H, Schlaefli HG, Keevil CW, Webb JS, Tews I. Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator. FEBS Lett. 2014 Dec 20;588(24):4631-6. doi: 10.1016/j.febslet.2014.11.002. Epub, 2014 Nov 11. PMID:25447517 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.002
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