4j40 | pdb_00004j40

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

spinqualitylabelsall models 4j40, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j40 is a 2 chain structure with sequence from Pseae. This structure supersedes the now removed PDB entry 3hvb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3hv8, 3hv9, 3hva Gene: fimX, PA4959 (PSEAE) Activity: Cyclic-guanylate-specific phosphodiesterase, with EC number 3.1.4.52 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.,Navarro MV, De N, Bae N, Wang Q, Sondermann H Structure. 2009 Aug 12;17(8):1104-16. PMID:19679088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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