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

Richard W. Meek, Ian T. Cadby, Patrick J. Moynihan and Andrew L. Lovering ()
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Richard W. Meek: University of Birmingham
Ian T. Cadby: University of Birmingham
Patrick J. Moynihan: University of Birmingham
Andrew L. Lovering: University of Birmingham

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-12051-6

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