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

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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)

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.

Suggested Citation

  • Richard W. Meek & Ian T. Cadby & Patrick J. Moynihan & Andrew L. Lovering, 2019. "Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12051-6
    DOI: 10.1038/s41467-019-12051-6
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