6qrj

Crystal structure of ShkA full-length in complex with AMPPNP

spinqualitylabelsall models 6qrj, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qrj is a 1 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: ANP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9ABT2_CAUVC Publication Abstract from PubMed Cytosolic hybrid histidine kinases (HHKs) constitute major signaling nodes that control various biological processes, but their input signals and how these are processed are largely unknown. In Caulobacter crescentus, the HHK ShkA is essential for accurate timing of the G1-S cell cycle transition and is regulated by the corresponding increase in the level of the second messenger c-di-GMP. Here, we use a combination of X-ray crystallography, NMR spectroscopy, functional analyses, and kinetic modeling to reveal the regulatory mechanism of ShkA. In the absence of c-di-GMP, ShkA predominantly adopts a compact domain arrangement that is catalytically inactive. C-di-GMP binds to the dedicated pseudoreceiver domain Rec1, thereby liberating the canonical Rec2 domain from its central position where it obstructs the large-scale motions required for catalysis. Thus, c-di-GMP cannot only stabilize domain interactions, but also engage in domain dissociation to allosterically invoke a downstream effect. Enzyme kinetics data are consistent with conformational selection of the ensemble of active domain constellations by the ligand and show that autophosphorylation is a reversible process. Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation.,Dubey BN, Agustoni E, Bohm R, Kaczmarczyk A, Mangia F, von Arx C, Jenal U, Hiller S, Plaza-Menacho I, Schirmer T Proc Natl Acad Sci U S A. 2019 Dec 27. pii: 1911427117. doi:, 10.1073/pnas.1911427117. PMID:31882446 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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