4J40

Crystal structure of the dual-domain GGDEF-EAL module of FimX from Pseudomonas aeruginosa

Replaces:  3HVB

Summary for 4J40

• Entry DOI: 10.2210/pdb4j40/pdb
• Related: 3HV8 3HV9 3HVA
• Descriptor: FimX (1 entity in total)
• Functional Keywords: eal phosphodiesterase, hydrolase, biofilm, c-di-gmp effector, c-di-gmp
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 95499.96

Authors

Navarro, M.V.,De, N.,Bae, N.,Wang, Q.,Sondermann, H. (deposition date: 2013-02-06, release date: 2013-02-20, Last modification date: 2024-02-28)

Primary citation

Navarro, M.V.,De, N.,Bae, N.,Wang, Q.,Sondermann, H.
Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.
Structure, 17:1104-1116, 2009

PubMed Abstract: Bacterial pathogenesis involves social behavior including biofilm formation and swarming, processes that are regulated by the bacterially unique second messenger cyclic di-GMP (c-di-GMP). Diguanylate cyclases containing GGDEF and phosphodiesterases containing EAL domains have been identified as the enzymes controlling cellular c-di-GMP levels, yet less is known regarding signal transmission and the targets of c-di-GMP. FimX, a protein from Pseudomonas aeruginosa that governs twitching motility, belongs to a large subfamily containing both GGDEF and EAL domains. Biochemical and structural analyses reveals its function as a high-affinity receptor for c-di-GMP. A model for full-length FimX was generated combining solution scattering data and crystal structures of the degenerate GGDEF and EAL domains. Although FimX forms a dimer in solution via the N-terminal domains, a crystallographic EAL domain dimer suggests modes for the regulation of FimX by c-di-GMP binding. The results provide the structural basis for c-di-GMP sensing via degenerate phosphodiesterases.

PubMed: 19679088
DOI: 10.1016/j.str.2009.06.010

Experimental method

X-RAY DIFFRACTION (2.99 Å)