Advertisement

Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime

  • Yuan Zhou
  • Xinghong Liu
  • Conggang Li
  • Maili Liu
  • Ling Jiang
  • Yixiang LiuEmail author
Article

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.

Keywords

Chemical shift assignment NMR HK853CA Secondary structure HSQC 

Notes

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).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. 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):213–224CrossRefGoogle Scholar
  2. Cai SJ, Inouye M (2002) EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J Biol Chem 277(27):24155–24161CrossRefGoogle Scholar
  3. Casino P, Rubio V, Marina A (2009) Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction. Cell 139(2):325–336CrossRefGoogle Scholar
  4. Chary KVR, Govil G (2008) NMR in biological systems: from molecules to human. Springer, DordrechtCrossRefGoogle Scholar
  5. 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 6:277–293CrossRefGoogle Scholar
  6. Foo YH, Gao Y, Zhang H, Kenney LJ (2015) Cytoplasmic sensing by the inner membrane histidine kinase EnvZ. Prog Biophys Mol Biol 118(3):119–129CrossRefGoogle Scholar
  7. Hoch JA (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3(2):165–170CrossRefGoogle Scholar
  8. 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 97:111–120CrossRefGoogle Scholar
  9. Laub MT, Goulian M (2007) Specificity in two-component signal transduction pathways. Annu Rev Genet 41:121–145CrossRefGoogle Scholar
  10. 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):2104ADSCrossRefGoogle Scholar
  11. Marina A, Waldburger CD, Hendrickson WA (2005) Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J 24(24):4247–4259CrossRefGoogle Scholar
  12. 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):1636–1647CrossRefGoogle Scholar
  13. Stock AM, Robinson VL, Goudreau PN (2000) Two-component signal transduction. Annu Rev Biochem 69:183–215CrossRefGoogle Scholar
  14. Thomason P, Kay R (2000) Eukaryotic signal transduction via histidine-aspartate phosphorelay. J Cell Sci 113(Pt 18):3141–3150Google Scholar
  15. Wilke KE, Francis S, Carlson EE (2015) Inactivation of multiple bacterial histidine kinases by targeting the ATP-binding domain. ACS Chem Biol 10(1):328–335CrossRefGoogle Scholar
  16. 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):e1003084CrossRefGoogle Scholar
  17. Wolanin PM, Webre DJ, Stock JB (2003) Mechanism of phosphatase activity in the chemotaxis response regulator CheY. Biochemistry 42(47):14075CrossRefGoogle Scholar
  18. 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):213–223CrossRefGoogle Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Key Laboratory of Magnetic Resonance in Biological Systems, National Center for Magnetic Resonance in Wuhan, State Key Laboratory of Magnetic Resonance and Atomic and Molecular PhysicsWuhan Institute of Physics and Mathematics, The Chinese Academy of SciencesWuhanChina
  2. 2.Graduate University of Chinese Academy of ScienceBeijingChina

Personalised recommendations