7cjr

Crystal structure of a periplasmic sensor domain of histidine kinase VbrK

spinqualitylabelsall models 7cjr, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cjr is a 1 chain structure with sequence from "oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, PEG Gene: CGJ74_25135, WR32_19055 ("Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961) Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacterial two-component regulatory systems (TCS) play important roles in sensing environmental stimuli and responding to them by regulating gene expression. VbrK/VbrR, a TCS in Vibrio parahaemolyticus, confers resistance to beta-lactam antibiotics through activating a beta-lactamase gene. Its periplasmic sensor domain was previously suggested to detect beta-lactam antibiotics by direct binding. Here, we report a crystal structure of the periplasmic sensing domain of VbrK (VbrK(SD)) using sulfur-based single-wavelength anomalous diffraction (S-SAD) phasing. Contrary to most bacterial sensor domains which form dimers, we show that VbrK(SD) is a monomer using size exclusion chromatography coupled with multi-angle light scattering. This observation is also supported by molecular dynamics simulations. To quantify the binding affinity of beta-lactam antibiotics to VbrK(SD), we performed isothermal titration calorimetry and other biophysical analyses. Unexpectedly, VbrK(SD) did not show any significant binding to beta-lactam antibiotics. Therefore, we propose that the detection of beta-lactam antibiotics by VbrK is likely to be indirect via an as yet unidentified mechanism. Crystal structure of the periplasmic sensor domain of histidine kinase VbrK suggests indirect sensing of beta-lactam antibiotics.,Goh BC, Chua YK, Qian X, Lin J, Savko M, Dedon PC, Lescar J J Struct Biol. 2020 Sep 2;212(2):107610. doi: 10.1016/j.jsb.2020.107610. PMID:32890780 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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