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4FOJ

1.55 A Crystal Structure of Xanthomonas citri FimX EAL domain in complex with c-diGMP

Summary for 4FOJ
Entry DOI10.2210/pdb4foj/pdb
Related3CNR 4FOK 4FOU
DescriptorFimX, 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) (3 entities in total)
Functional Keywordstim like barrel, beta-(beta/alpha)6-beta, c-di-gmp binding, type iv pilus assembly, pilz, protein binding
Biological sourceXanthomonas axonopodis pv. citri
Total number of polymer chains1
Total formula weight30302.86
Authors
Farah, C.S.,Guzzo, C.R. (deposition date: 2012-06-20, release date: 2013-03-27, Last modification date: 2024-02-28)
Primary citationGuzzo, C.R.,Dunger, G.,Salinas, R.K.,Farah, C.S.
Structure of the PilZ-FimXEAL-c-di-GMP Complex Responsible for the Regulation of Bacterial Type IV Pilus Biogenesis.
J.Mol.Biol., 425:2174-2197, 2013
Cited by
PubMed Abstract: 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 β-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.
PubMed: 23507310
DOI: 10.1016/j.jmb.2013.03.021
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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