6kkp

The crystal structure of apo-SiaC from Pseudomonas aeruginosa

spinqualitylabelsall models 6kkp, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kkp is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I6W2_PSEAE Publication Abstract from PubMed Bacterial cyclic-di-GMP (c-di-GMP) production is associated with biofilm development and the switch from acute to chronic infections. In Pseudomonas aeruginosa, the diguanylate cyclase (DGC) SiaD and phosphatase SiaA, which are co-transcribed as part of a siaABCD operon, are essential for cellular aggregation. However, the detailed functions of this operon and the relationships among its constituent genes are unknown. Here, we demonstrate that the siaABCD operon encodes for a signaling network that regulates SiaD enzymatic activity to control biofilm and aggregates formation. Through protein-protein interaction, SiaC promotes SiaD diguanylate cyclase activity. Biochemical and structural data revealed that SiaB is an unusual protein kinase that phosphorylates SiaC, whereas SiaA phosphatase can dephosphorylate SiaC. The phosphorylation state of SiaC is critical for its interaction with SiaD, which will switch on or off the DGC activity of SiaD and regulate c-di-GMP levels and subsequent virulence phenotypes. Collectively, our data provide insights into the molecular mechanisms underlying the modulation of DGC activity associated with chronic infections, which may facilitate the development of antimicrobial drugs. The SiaA/B/C/D signaling network regulates biofilm formation in Pseudomonas aeruginosa.,Chen G, Gan J, Yang C, Zuo Y, Peng J, Li M, Huo W, Xie Y, Zhang Y, Wang T, Deng X, Liang H EMBO J. 2020 Mar 16;39(6):e103412. doi: 10.15252/embj.2019103412. Epub 2020 Feb, 24. PMID:32090355 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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