3HVA

Crystal structure of FimX GGDEF domain from Pseudomonas aeruginosa

Summary for 3HVA

• Entry DOI: 10.2210/pdb3hva/pdb
• Related: 3HV8 3HV9 3HVB
• Descriptor: Protein FimX (2 entities in total)
• Functional Keywords: ggdef diguanylate cyclase, biofilm, c-di-gmp, transferase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 2
• Total formula weight: 38265.12

Authors

Navarro, M.V.A.S.,De, N.,Bae, N.,Sondermann, H. (deposition date: 2009-06-15, release date: 2009-08-18, Last modification date: 2023-09-06)

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 (2.042 Å)