Org Domain
The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)2 at the active site (Med Worm)
Cyclic diguanosine monophosphate (c-di-GMP) is a key signalling molecule
involved in regulating many important biological functions in bacteria. The
synthesis of c-di-GMP is catalyzed by the GGDEF-domain-containing diguanylate
cyclase (DGC), the activity of which is regulated by the binding of product at
the allosteric inhibitory (I) site. However, a significant number of GGDEF
domains lack the RxxD motif characteristic of the allosteric I site. Here, the
structure of XCC4471GGDEF, the GGDEF domain of a DGC from Xanthomonas
campestris, in complex with c-di-GMP has been solved. Unexpectedly, the
structure of the complex revealed a GGDEF-domain dimer cross-linked by two
molecules of c-di-GMP at the strongly conserved active sites. In the complex
(c-di-GMP)2 adopts a novel partially interca...
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