6HC1

Bdellovibrio bacteriovorus DgcB FHA in complex with phosphorylated N-terminal peptide

Summary for 6HC1

• Entry DOI: 10.2210/pdb6hc1/pdb
• Related: 6HBZ 6HC0
• Descriptor: GGDEF domain protein, DgcB N-terminus, phosphorylated (3 entities in total)
• Functional Keywords: ggdef, fha, c-di-gmp, diguanylate cyclase, signaling protein
• Biological source: Bdellovibrio bacteriovorus HD100; More
• Total number of polymer chains: 3
• Total formula weight: 23175.51

Authors

Lovering, A.L.,Meek, R.W. (deposition date: 2018-08-13, release date: 2019-08-28, Last modification date: 2019-11-06)

Primary citation

Meek, R.W.,Cadby, I.T.,Moynihan, P.J.,Lovering, A.L.
Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio.
Nat Commun, 10:4086-4086, 2019

PubMed 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.

PubMed: 31501441
DOI: 10.1038/s41467-019-12051-6

Experimental method

X-RAY DIFFRACTION (1.49 Å)