6HBZ

Bdellovibrio bacteriovorus DgcB Full-length

Summary for 6HBZ

• Entry DOI: 10.2210/pdb6hbz/pdb
• Descriptor: GGDEF domain protein, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: ggdef, fha, c-di-gmp, diguanylate cyclase, signaling protein
• Biological source: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
• Total number of polymer chains: 2
• Total formula weight: 62719.75

Authors

Lovering, A.L.,Meek, R.W. (deposition date: 2018-08-13, release date: 2019-08-28, Last modification date: 2024-05-15)

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 (1.79 Å)