Receiver domain of sensor histidine kinase CKI1
From Proteopedia
![]() Receiver domain of CKI1 from Arabidopsis, 3mmn
Receiver domain of sensor histidine kinase CKI1 (CKI1RD) catalyses the transphosphorylation reaction during hormonal and abiotic signalling in plants. Membrane-bound histidine kinase Cytokinin-independet 1 (CKI1) is a member of the Multistep phosphorelay (MSP) signalling pathway in Arabidopsis. CKI1 was found to be constitutively active activator of a cytokinin-like response. Intracellularly located C-terminal CKI1RD is responsible for the recognition of CKI1 downstream signalling partners from family of Arabidopsis histidine-containing phosphotransfer proteins (AHP) and triggers the cytokinin-like signal transmission. Divalent magnesium ion bound in the active site of CKI1RD is essential for the transphosphorylation reaction. Crystal structure of CKI1RD was determined as magnesium-free and magnesium-bound form. Magnesium binding induces the rearrangement of residues around the active site of CKI1RD, as was determined by both X-ray crystallography and NMR spectroscopy. Biological FunctionCKI1 as member of Multistep phosphorelay signaling in Arabidopsis CKI1RD structure and effects of magnesium binding in the active siteThe crystal structure of CKI1RD shows the conformational conservation of RDs belonging to CheY-like protein superfamily [14][15]. CKI1RD is folded in a (α/β)5 manner with central β-sheet formed from parallel beta-strands (β2-β1-β3-β4-β5) surrounded on both sides by two (α1 and α5) and three (α2, α3, α4) α-helices. Secondary structure elements are connected by five loops L1-L5 on the face side of the protein. The active site with phosphoacceptor D1050 is located at the C-termini of the central β3-strand in a pocket delineated loops L1, L3 and L5. A highly conserved triad of carboxyl oxygens, formed by D1050 together with D992 and D993 and carbonyl oxygen of Q1052 give the active site an acidic character. This architecture of the active site is well conserved among CheY-like superfamily and corresponds to the phosphotransfer function of the receiver domains. -restore original scene- ![]() (a) Magnesium-free and (b)magnesium-bound forms of the CKI1RD active site. Magnesium ion (magenta) is approximately octahedrally coordinated. (c) 2Fo-Fc omit map of CKI1RD magnesium bound contoured at 1σ. Conservation of the structure and sequence among known receiver domains. The magnesium ion and all atoms in radius of 5Å were omitted from phasing. |
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3D Structures of CKI1RD and similar receiver domains
3mm4 - CKI1RD in metal free form
3mmn - CKI1RD in magnesium bound form
3dcf - ETR1RD, receiver domain of plant hormone ethylene receptor from Arabidopsis
2chy - CheY, chemotaxis response regulatory protein from Salmonella enterica
3dgf - response regulatory signalling protein from Thermotoga maritina
References
- ↑ Kakimoto T. CKI1, a histidine kinase homolog implicated in cytokinin signal transduction. Science. 1996 Nov 8;274(5289):982-5. PMID:8875940
- ↑ Pischke MS, Jones LG, Otsuga D, Fernandez DE, Drews GN, Sussman MR. An Arabidopsis histidine kinase is essential for megagametogenesis. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15800-5. Epub 2002 Nov 8. PMID:12426401 doi:10.1073/pnas.232580499
- ↑ Hejatko J, Pernisova M, Eneva T, Palme K, Brzobohaty B. The putative sensor histidine kinase CKI1 is involved in female gametophyte development in Arabidopsis. Mol Genet Genomics. 2003 Jul;269(4):443-53. Epub 2003 May 28. PMID:12774227 doi:10.1007/s00438-003-0858-7
- ↑ Brenner WG, Ramireddy E, Heyl A, Schmulling T. Gene regulation by cytokinin in Arabidopsis. Front Plant Sci. 2012;3:8. Epub 2012 Jan 31. PMID:22639635 doi:10.3389/fpls.2012.00008
- ↑ Yamada H, Suzuki T, Terada K, Takei K, Ishikawa K, Miwa K, Yamashino T, Mizuno T. The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that transduces cytokinin signals across the membrane. Plant Cell Physiol. 2001 Sep;42(9):1017-23. PMID:11577198
- ↑ Hwang I, Sheen J. Two-component circuitry in Arabidopsis cytokinin signal transduction. Nature. 2001 Sep 27;413(6854):383-9. PMID:11574878 doi:10.1038/35096500
- ↑ Urao T, Yamaguchi-Shinozaki K, Shinozaki K. Two-component systems in plant signal transduction. Trends Plant Sci. 2000 Feb;5(2):67-74. PMID:10664616
- ↑ Mount SM, Chang C. Evidence for a plastid origin of plant ethylene receptor genes. Plant Physiol. 2002 Sep;130(1):10-4. PMID:12226482 doi:10.1104/pp.005397
- ↑ Heyl A, Schmulling T. Cytokinin signal perception and transduction. Curr Opin Plant Biol. 2003 Oct;6(5):480-8. PMID:12972049
- ↑ Urao T, Miyata S, Yamaguchi-Shinozaki K, Shinozaki K. Possible His to Asp phosphorelay signaling in an Arabidopsis two-component system. FEBS Lett. 2000 Aug 4;478(3):227-32. PMID:10930573
- ↑ Dortay H, Mehnert N, Burkle L, Schmulling T, Heyl A. Analysis of protein interactions within the cytokinin-signaling pathway of Arabidopsis thaliana. FEBS J. 2006 Oct;273(20):4631-44. Epub 2006 Sep 11. PMID:16965536 doi:10.1111/j.1742-4658.2006.05467.x
- ↑ Dortay H, Gruhn N, Pfeifer A, Schwerdtner M, Schmulling T, Heyl A. Toward an interaction map of the two-component signaling pathway of Arabidopsis thaliana. J Proteome Res. 2008 Sep;7(9):3649-60. Epub 2008 Jul 22. PMID:18642946 doi:10.1021/pr0703831
- ↑ Pekarova B, Klumpler T, Triskova O, Horak J, Jansen S, Dopitova R, Papouskova V, Nejedla E, Sklenar V, Marek J, Zidek L, Hejatko J, Janda L. Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. Plant J. 2011 May 13. doi: 10.1111/j.1365-313X.2011.04637.x. PMID:21569135 doi:10.1111/j.1365-313X.2011.04637.x
- ↑ Stock AM, Martinez-Hackert E, Rasmussen BF, West AH, Stock JB, Ringe D, Petsko GA. Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry. 1993 Dec 14;32(49):13375-80. PMID:8257674
- ↑ Wilson D, Pethica R, Zhou Y, Talbot C, Vogel C, Madera M, Chothia C, Gough J. SUPERFAMILY--sophisticated comparative genomics, data mining, visualization and phylogeny. Nucleic Acids Res. 2009 Jan;37(Database issue):D380-6. Epub 2008 Nov 26. PMID:19036790 doi:10.1093/nar/gkn762
- ↑ Pekarova B, Klumpler T, Triskova O, Horak J, Jansen S, Dopitova R, Papouskova V, Nejedla E, Sklenar V, Marek J, Zidek L, Hejatko J, Janda L. Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. Plant J. 2011 May 13. doi: 10.1111/j.1365-313X.2011.04637.x. PMID:21569135 doi:10.1111/j.1365-313X.2011.04637.x