Abstract
HK853 is a transmembrane protein from Thermotoga maritime, which belongs to HK853/RR468 two-component signal transduction system (TCS) and acts as a sensor histidine kinase. HK853 is mainly composed of a transmembrane domain, dimerization and histidine-containing phosphotransfer domain (HK853DHp), catalytic and ATP-binding domain (HK853CA) and several linkers. HK853 can be completely autophosphorylated, which is the first step for signal transduction of TCS. HK853CA is an essential domain for its kinase function, since HK853CA could bind with ATP and convert it to ADP. Here, we report the backbone and part of side chain assignments of HK853CA. By analyzing the chemical shifts of HN, N, CO, Cα and Cβ, the secondary structure was predicted and contrasted with the published crystal structure of HK853CA. The result showed that our predicted structure could basically fit into the crystal structure. Thus, the chemical shift assignments of HK853CA are the starting point for further structural and dynamics study.
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References
Bem AE, Velikova N, Pellicer MT, Baarlen PV, Marina A, Wells JM (2015) Bacterial histidine kinases as novel antibacterial drug targets. ACS Chem Biol 10(1):213–224
Cai SJ, Inouye M (2002) EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J Biol Chem 277(27):24155–24161
Casino P, Rubio V, Marina A (2009) Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction. Cell 139(2):325–336
Chary KVR, Govil G (2008) NMR in biological systems: from molecules to human. Springer, Dordrecht
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Foo YH, Gao Y, Zhang H, Kenney LJ (2015) Cytoplasmic sensing by the inner membrane histidine kinase EnvZ. Prog Biophys Mol Biol 118(3):119–129
Hoch JA (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3(2):165–170
Jacobs C, Domian IJ, Maddock JR, Shapiro L (1999) Cell cycle-dependent polar localization of an essential bacterial histidine kinase that controls DNA replication and cell division. Cell 97:111–120
Laub MT, Goulian M (2007) Specificity in two-component signal transduction pathways. Annu Rev Genet 41:121–145
Liu Y, Rose J, Huang S, Hu Y, Wu Q, Wang D, Li C, Liu M, Zhou P, Jiang L (2017) A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases. Nat Commun 8(1):2104
Marina A, Waldburger CD, Hendrickson WA (2005) Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J 24(24):4247–4259
Podgornaia AI, Casino P, Marina A, Laub MT (2013) Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling. Structure 21(9):1636–1647
Stock AM, Robinson VL, Goudreau PN (2000) Two-component signal transduction. Annu Rev Biochem 69:183–215
Thomason P, Kay R (2000) Eukaryotic signal transduction via histidine-aspartate phosphorelay. J Cell Sci 113(Pt 18):3141–3150
Wilke KE, Francis S, Carlson EE (2015) Inactivation of multiple bacterial histidine kinases by targeting the ATP-binding domain. ACS Chem Biol 10(1):328–335
Willett JW, Kirby JR (2012) Genetic and biochemical dissection of a HisKA domain identifies residues required exclusively for kinase and phosphatase activities. PLoS Genet 8(11):e1003084
Wolanin PM, Webre DJ, Stock JB (2003) Mechanism of phosphatase activity in the chemotaxis response regulator CheY. Biochemistry 42(47):14075
Yang S, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213–223
Acknowledgements
This project was supported by Grants from National Key R&D Program of China (#2017YFA0505400) and the Natural Science Foundation of China (#21573280 and #21603268).
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Zhou, Y., Liu, X., Li, C. et al. Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime. Biomol NMR Assign 13, 173–176 (2019). https://doi.org/10.1007/s12104-019-09872-3
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DOI: https://doi.org/10.1007/s12104-019-09872-3