4f3h | pdb_00004f3h

The structural of FimXEAL-c-di-GMP from Xanthomonas campestris

spinqualitylabelsall models 4f3h, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f3h is a 1 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: C2E Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8P8F1_XANCP Publication Abstract from PubMed 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. Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein.,Chin KH, Kuo WT, Yu YJ, Liao YT, Yang MT, Chou SH Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1380-92. doi:, 10.1107/S0907444912030594. Epub 2012 Sep 18. PMID:22993092 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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