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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.