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Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio

Nature Communications, ISSN: 2041-1723, Vol: 10, Issue: 1, Page: 4086
2019
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Study reveals the attack initiation mechanism of predatory bacteria

Scientists have unraveled the attack initiation mechanism used by so-called "predatory bacteria', which are capable of invading and killing harmful bugs including E. coli or Salmonella.

Article Description

The bacterial second messenger cyclic-di-GMP is a widespread, prominent effector of lifestyle change. An example of this occurs in the predatory bacterium Bdellovibrio bacteriovorus, which cycles between free-living and intraperiplasmic phases after entering (and killing) another bacterium. The initiation of prey invasion is governed by DgcB (GGDEF enzyme) that produces cyclic-di-GMP in response to an unknown stimulus. Here, we report the structure of DgcB, and demonstrate that the GGDEF and sensory forkhead-associated (FHA) domains form an asymmetric dimer. Our structures indicate that the FHA domain is a consensus phosphopeptide sensor, and that the ligand for activation is surprisingly derived from the N-terminal region of DgcB itself. We confirm this hypothesis by determining the structure of a FHA:phosphopeptide complex, from which we design a constitutively-active mutant (confirmed via enzyme assays). Our results provide an understanding of the stimulus driving DgcB-mediated prey invasion and detail a unique mechanism of GGDEF enzyme regulation.

Bibliographic Details

Richard W. Meek; Ian T. Cadby; Patrick J. Moynihan; Andrew L. Lovering

Springer Science and Business Media LLC

Chemistry; Biochemistry, Genetics and Molecular Biology; Physics and Astronomy

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