6HQ5

Structure of EAL Enzyme Bd1971 - cAMP and cyclic-di-GMP bound form

Summary for 6HQ5

• Entry DOI: 10.2210/pdb6hq5/pdb
• Related: 6HQ2 6HQ3 6HQ4
• Descriptor: EAL Enzyme Bd1971, 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), ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, ... (5 entities in total)
• Functional Keywords: eal, cyclic-di-gmp, camp, bdellovibrio, signaling protein
• Biological source: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
• Total number of polymer chains: 2
• Total formula weight: 91958.55

Authors

Lovering, A.L.,Cadby, I.T. (deposition date: 2018-09-24, release date: 2019-07-31, Last modification date: 2024-05-01)

Primary citation

Cadby, I.T.,Basford, S.M.,Nottingham, R.,Meek, R.,Lowry, R.,Lambert, C.,Tridgett, M.,Till, R.,Ahmad, R.,Fung, R.,Hobley, L.,Hughes, W.S.,Moynihan, P.J.,Sockett, R.E.,Lovering, A.L.
Nucleotide signaling pathway convergence in a cAMP-sensing bacterial c-di-GMP phosphodiesterase.
Embo J., 38:e100772-e100772, 2019

PubMed Abstract: Bacterial usage of the cyclic dinucleotide c-di-GMP is widespread, governing the transition between motile/sessile and unicellular/multicellular behaviors. There is limited information on c-di-GMP metabolism, particularly on regulatory mechanisms governing control of EAL c-di-GMP phosphodiesterases. Herein, we provide high-resolution structures for an EAL enzyme Bd1971, from the predatory bacterium Bdellovibrio bacteriovorus, which is controlled by a second signaling nucleotide, cAMP. The full-length cAMP-bound form reveals the sensory N-terminus to be a domain-swapped variant of the cNMP/CRP family, which in the cAMP-activated state holds the C-terminal EAL enzyme in a phosphodiesterase-active conformation. Using a truncation mutant, we trap both a half-occupied and inactive apo-form of the protein, demonstrating a series of conformational changes that alter juxtaposition of the sensory domains. We show that Bd1971 interacts with several GGDEF proteins (c-di-GMP producers), but mutants of Bd1971 do not share the discrete phenotypes of GGDEF mutants, instead having an elevated level of c-di-GMP, suggesting that the role of Bd1971 is to moderate these levels, allowing "action potentials" to be generated by each GGDEF protein to effect their specific functions.

PubMed: 31355487
DOI: 10.15252/embj.2018100772

Experimental method

X-RAY DIFFRACTION (2.83 Å)