Journal
FEBS LETTERS
Volume 588, Issue 24, Pages 4631-4636Publisher
WILEY
DOI: 10.1016/j.febslet.2014.11.002
Keywords
Motility regulator A; Diguanylate cyclases; Phosphodiesterases; Cyclic dimeric guanosine monophosphate; Biofilm dispersal
Funding
- BBSRC
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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. (C) 2014 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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