4fou | pdb_00004fou

Structure of the PilZ-FimX(EAL domain)-c-di-GMP complex responsible for the regulation of bacterial Type IV pilus biogenesis

spinqualitylabelsall models 4fou, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fou is a 4 chain structure with sequence from Xanthomonas axonopodis pv. citri str. 306. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C2E, CA, GOL Related: 3cnr, 4foj, 4fok Gene: XAC2398 (Xanthomonas axonopodis pv. citri str. 306), pilZ, XAC1133 (Xanthomonas axonopodis pv. citri str. 306) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Signal transduction pathways mediated by cyclic-bis(3'-->5')-dimeric GMP (c-di-GMP) control many important and complex behaviors in bacteria. C-di-GMP is synthesized through the action of GGDEF domains that possess diguanylate cyclase activity and is degraded by EAL or HD-GYP domains with phosphodiesterase activity. There is mounting evidence that some important c-di-GMP-mediated pathways require protein-protein interactions between members of the GGDEF, EAL, HD-GYP and PilZ protein domain families. For example, interactions have been observed between PilZ and the EAL domain from FimX of Xanthomonas citri (Xac). FimX and PilZ are involved in the regulation of type IV pilus biogenesis via interactions of the latter with the hexameric PilB ATPase associated with the bacterial inner membrane. Here, we present the crystal structure of the ternary complex made up of PilZ, the FimX EAL domain (FimXEAL) and c-di-GMP. PilZ interacts principally with the lobe region and the N-terminal linker helix of the FimXEAL. These interactions involve a hydrophobic surface made up of amino acids conserved in a non-canonical family of PilZ domains that lack intrinsic c-di-GMP binding ability and strand complementation that joins beta-sheets from both proteins. Interestingly, the c-di-GMP binds to isolated FimXEAL and to the PilZ-FimXEAL complex in a novel conformation encountered in c-di-GMP-protein complexes in which one of the two glycosidic bonds is in a rare syn conformation while the other adopts the more common anti conformation. The structure points to a means by which c-di-GMP and PilZ binding could be coupled to FimX and PilB conformational states. Structure of the PilZ-FimX-c-di-GMP Complex Responsible for the Regulation of Bacterial Type IV Pilus Biogenesis.,Guzzo CR, Dunger G, Salinas RK, Farah CS J Mol Biol. 2013 Mar 16. pii: S0022-2836(13)00169-1. doi:, 10.1016/j.jmb.2013.03.021. PMID:23507310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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