4F48

The X-ray structural of FimXEAL-c-di-GMP-PilZ complexes from Xanthomonas campestris

Summary for 4F48

• Entry DOI: 10.2210/pdb4f48/pdb
• Related: 4F3H
• Descriptor: Putative uncharacterized protein, Type IV fimbriae assembly protein, 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), ... (4 entities in total)
• Functional Keywords: fimxeal-c-di-gmp-pilz complex, type iv pilus, signaling protein
• Biological source: Xanthomonas campestris pv. campestris; More
• Total number of polymer chains: 2
• Total formula weight: 41198.59

Authors

Chin, K.-H.,Liao, Y.-T.,Chou, S.-H. (deposition date: 2012-05-10, release date: 2012-11-14, Last modification date: 2024-03-20)

Primary citation

Chin, K.-H.,Kuo, W.-T.,Yu, Y.-J.,Liao, Y.-T.,Yang, M.T.,Chou, S.-H.
Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein.
Acta Crystallogr.,Sect.D, 68:1380-1392, 2012

PubMed Abstract: Cyclic di-GMP (c-di-GMP) is a novel secondary-messenger molecule that is involved in regulating a plethora of important bacterial activities through binding to an unprecedented array of effectors. Proteins with a canonical PilZ domain that bind c-di-GMP play crucial roles in regulating flagellum-based motility. In contrast, noncanonical type II PilZ domains that do not effectively bind c-di-GMP regulate twitching motility, which is dependent on type IV pili (T4P). Recent data indicate that T4P biogenesis is initiated via the interaction of a noncanonical type II PilZ protein with the GGDEF/EAL-domain protein FimX and the pilus motor protein PilB at high c-di-GMP concentrations. However, the molecular details of such interactions remain to be elucidated. In this manuscript, the first hetero-complex crystal structure between a type II PilZ protein and the EAL domain of the FimX protein (FimX(EAL)) from Xanthomonas campestris pv. campestris (Xcc) in the presence of c-di-GMP is reported. This work reveals two novel conformations of monomeric c-di-GMP in the XccFimX(EAL)-c-di-GMP and XccFimX(EAL)-c-di-GMP-XccPilZ complexes, as well as a unique interaction mode of a type II PilZ domain with FimX(EAL). These findings indicate that c-di-GMP is sufficiently flexible to adjust its conformation to match the corresponding recognition motifs of different cognate effectors. Together, these results represent a first step towards an understanding of how T4P biogenesis is controlled by c-di-GMP at the molecular level and also of the ability of c-di-GMP to bind to a wide variety of effectors.

PubMed: 22993092
DOI: 10.1107/S0907444912030594

Experimental method

X-RAY DIFFRACTION (3 Å)