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4rnj
From Proteopedia
(Difference between revisions)
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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=4rnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rnj RCSB], [http://www.ebi.ac.uk/pdbsum/4rnj PDBsum]</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=4rnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rnj RCSB], [http://www.ebi.ac.uk/pdbsum/4rnj PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25447517</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:14, 22 April 2015
PaMorA phosphodiesterase domain, apo form
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