5lnm

From Proteopedia

(Difference between revisions)

Revision as of 12:24, 17 July 2019

Crystal structure of D1050E mutant of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana

Structural highlights

5lnm is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	CKI1, At2g47430, T30B22.27 (ARATH)
Activity:	Histidine kinase, with EC number 2.7.13.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CKI1_ARATH] Essential protein. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Required for the development of megagametophyte in female gametophyte (embryo sac) independently of cytokinin. Contributes to vascular bundle formation and secondary growth in a cytokinin-independent manner, probably by promoting the maintenance of mitotic activity and/or identity of procambial cells. Seems to influence and promote the cytokinin signaling pathway.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Multistep phosphorelay (MSP) cascades mediate responses to a wide spectrum of stimuli, including plant hormonal signaling, but several aspects of MSP await elucidation. Here, we provide first insight into the key step of MSP-mediated phosphotransfer in a eukaryotic system, the phosphorylation of the receiver domain of the histidine kinase CYTOKININ INDEPENDENT 1 (CKI1RD) from Arabidopsis thaliana We observed that the crystal structures of free, Mg2+-bound, and beryllofluoridated CKI1RD (a stable analog of the labile phosphorylated form) were identical and similar to the active state of receiver domains of bacterial response regulators. However, the three CKI1RD variants exhibited different conformational dynamics in solution. NMR studies revealed that Mg2+ binding and beryllofluoridation alter the conformational equilibrium of the beta3-alpha3 loop close to the phosphorylation site. Mutations that perturbed the conformational behavior of the beta3-alpha3 loop while keeping the active site aspartate intact resulted in suppression of CKI1 function. Mechanistically, homology modeling indicated that the beta3-alpha3 loop directly interacts with the ATP-binding site of the CKI1 histidine kinase domain. The functional relevance of the conformational dynamics observed in the beta3-alpha3 loop of CKI1RD was supported by a comparison with another A. thaliana histidine kinase, ETR1. In contrast to the highly dynamic beta3-alpha3 loop of CKI1RD, the corresponding loop of the ETR1 receiver domain (ETR1RD) exhibited little conformational exchange and adopted a different orientation in crystals. Biochemical data indicated that ETR1RD is involved in phosphorylation-independent signaling, implying a direct link between conformational behavior and the ability of eukaryotic receiver domains to participate in MSP.

Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.,Otrusinova O, Demo G, Padrta P, Jasenakova Z, Pekarova B, Gelova Z, Szmitkowska A, Kaderavek P, Jansen S, Zachrdla M, Klumpler T, Marek J, Hritz J, Janda L, Iwai H, Wimmerova M, Hejatko J, Zidek L J Biol Chem. 2017 Aug 31. pii: jbc.M117.790212. doi: 10.1074/jbc.M117.790212. PMID:28860196^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakamura A, Kakimoto T, Imamura A, Suzuki T, Ueguchi C, Mizuno T. Biochemical characterization of a putative cytokinin-responsive His-kinase, CKI1, from Arabidopsis thaliana. Biosci Biotechnol Biochem. 1999 Sep;63(9):1627-30. PMID:10610126
↑ 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
↑ Tran LS, Urao T, Qin F, Maruyama K, Kakimoto T, Shinozaki K, Yamaguchi-Shinozaki K. Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases in response to abscisic acid, drought, and salt stress in Arabidopsis. Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20623-8. Epub 2007 Dec 12. PMID:18077346 doi:http://dx.doi.org/10.1073/pnas.0706547105
↑ Hejatko J, Ryu H, Kim GT, Dobesova R, Choi S, Choi SM, Soucek P, Horak J, Pekarova B, Palme K, Brzobohaty B, Hwang I. The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS HISTIDINE KINASE2 and 3 regulate vascular tissue development in Arabidopsis shoots. Plant Cell. 2009 Jul;21(7):2008-21. doi: 10.1105/tpc.109.066696. Epub 2009 Jul, 21. PMID:19622803 doi:http://dx.doi.org/10.1105/tpc.109.066696
↑ Deng Y, Dong H, Mu J, Ren B, Zheng B, Ji Z, Yang WC, Liang Y, Zuo J. Arabidopsis histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth. Plant Cell. 2010 Apr;22(4):1232-48. doi: 10.1105/tpc.108.065128. Epub 2010 Apr 2. PMID:20363773 doi:http://dx.doi.org/10.1105/tpc.108.065128
↑ Kakimoto T. CKI1, a histidine kinase homolog implicated in cytokinin signal transduction. Science. 1996 Nov 8;274(5289):982-5. PMID:8875940
↑ Otrusinova O, Demo G, Padrta P, Jasenakova Z, Pekarova B, Gelova Z, Szmitkowska A, Kaderavek P, Jansen S, Zachrdla M, Klumpler T, Marek J, Hritz J, Janda L, Iwai H, Wimmerova M, Hejatko J, Zidek L. Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana. J Biol Chem. 2017 Aug 31. pii: jbc.M117.790212. doi: 10.1074/jbc.M117.790212. PMID:28860196 doi:http://dx.doi.org/10.1074/jbc.M117.790212

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lnm"

@@ Line 1: / Line 1: @@
 ==Crystal structure of D1050E mutant of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana==
-<StructureSection load='5lnm' size='340' side='right' caption='[[5lnm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='5lnm' size='340' side='right'caption='[[5lnm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lnm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LNM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lnm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LNM FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKI1, At2g47430, T30B22.27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnm OCA], [http://pdbe.org/5lnm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lnm RCSB], [http://www.ebi.ac.uk/pdbsum/5lnm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnm ProSAT]</span></td></tr>
 </table>
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Arath]]
 [[Category: Histidine kinase]]
+[[Category: Large Structures]]
 [[Category: Demo, G]]
 [[Category: Hejatko, J]]

5lnm

From Proteopedia

Revision as of 12:24, 17 July 2019

Crystal structure of D1050E mutant of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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