4ebz

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Crystal structure of the ectodomain of a receptor like kinase

Structural highlights

4ebz is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.792Å
Ligands:BMA, MAN, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CERK1_ARATH Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI).[1] [2] [3] [4] [5] [6] [7] [8]

Publication Abstract from PubMed

Pattern recognition receptors confer plant resistance to pathogen infection by recognizing the conserved pathogen-associated molecular patterns. The cell surface receptor chitin elicitor receptor kinase 1 of Arabidopsis (AtCERK1) directly binds chitin through its lysine motif (LysM)-containing ectodomain (AtCERK1-ECD) to activate immune responses. The crystal structure that we solved of an AtCERK1-ECD complexed with a chitin pentamer reveals that their interaction is primarily mediated by a LysM and three chitin residues. By acting as a bivalent ligand, a chitin octamer induces AtCERK1-ECD dimerization that is inhibited by shorter chitin oligomers. A mutation attenuating chitin-induced AtCERK1-ECD dimerization or formation of nonproductive AtCERK1 dimer by overexpression of AtCERK1-ECD compromises AtCERK1-mediated signaling in plant cells. Together, our data support the notion that chitin-induced AtCERK1 dimerization is critical for its activation.

Chitin-induced dimerization activates a plant immune receptor.,Liu T, Liu Z, Song C, Hu Y, Han Z, She J, Fan F, Wang J, Jin C, Chang J, Zhou JM, Chai J Science. 2012 Jun 1;336(6085):1160-4. PMID:22654057[9]

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

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Citations
108 reviews cite this structure
Speak, friend, and enter: signalling systems that promote beneficial symbiotic associations in plants.
Oldroyd et al. (2013)
107 more
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References

  1. ↑ Miya A, Albert P, Shinya T, Desaki Y, Ichimura K, Shirasu K, Narusaka Y, Kawakami N, Kaku H, Shibuya N. CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19613-8. Epub 2007 Nov 27. PMID:18042724 doi:http://dx.doi.org/10.1073/pnas.0705147104
  2. ↑ Wan J, Zhang XC, Neece D, Ramonell KM, Clough S, Kim SY, Stacey MG, Stacey G. A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis. Plant Cell. 2008 Feb;20(2):471-81. doi: 10.1105/tpc.107.056754. Epub 2008 Feb 8. PMID:18263776 doi:http://dx.doi.org/10.1105/tpc.107.056754
  3. ↑ Gimenez-Ibanez S, Hann DR, Ntoukakis V, Petutschnig E, Lipka V, Rathjen JP. AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants. Curr Biol. 2009 Mar 10;19(5):423-9. doi: 10.1016/j.cub.2009.01.054. Epub 2009 Feb, 26. PMID:19249211 doi:http://dx.doi.org/10.1016/j.cub.2009.01.054
  4. ↑ Gimenez-Ibanez S, Ntoukakis V, Rathjen JP. The LysM receptor kinase CERK1 mediates bacterial perception in Arabidopsis. Plant Signal Behav. 2009 Jun;4(6):539-41. doi: 10.1016/j.cub.2009.01.054. Epub, 2009 Jun 8. PMID:19816132 doi:http://dx.doi.org/10.1016/j.cub.2009.01.054
  5. ↑ Petutschnig EK, Jones AM, Serazetdinova L, Lipka U, Lipka V. The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation. J Biol Chem. 2010 Sep 10;285(37):28902-11. doi: 10.1074/jbc.M110.116657. Epub, 2010 Jul 7. PMID:20610395 doi:http://dx.doi.org/10.1074/jbc.M110.116657
  6. ↑ Willmann R, Lajunen HM, Erbs G, Newman MA, Kolb D, Tsuda K, Katagiri F, Fliegmann J, Bono JJ, Cullimore JV, Jehle AK, Gotz F, Kulik A, Molinaro A, Lipka V, Gust AA, Nurnberger T. Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection. Proc Natl Acad Sci U S A. 2011 Dec 6;108(49):19824-9. doi:, 10.1073/pnas.1112862108. Epub 2011 Nov 21. PMID:22106285 doi:http://dx.doi.org/10.1073/pnas.1112862108
  7. ↑ Brotman Y, Landau U, Pnini S, Lisec J, Balazadeh S, Mueller-Roeber B, Zilberstein A, Willmitzer L, Chet I, Viterbo A. The LysM receptor-like kinase LysM RLK1 is required to activate defense and abiotic-stress responses induced by overexpression of fungal chitinases in Arabidopsis plants. Mol Plant. 2012 Sep;5(5):1113-24. doi: 10.1093/mp/sss021. Epub 2012 Mar 28. PMID:22461667 doi:http://dx.doi.org/10.1093/mp/sss021
  8. ↑ Shinya T, Motoyama N, Ikeda A, Wada M, Kamiya K, Hayafune M, Kaku H, Shibuya N. Functional characterization of CEBiP and CERK1 homologs in arabidopsis and rice reveals the presence of different chitin receptor systems in plants. Plant Cell Physiol. 2012 Oct;53(10):1696-706. doi: 10.1093/pcp/pcs113. Epub 2012 , Aug 13. PMID:22891159 doi:http://dx.doi.org/10.1093/pcp/pcs113
  9. ↑ Liu T, Liu Z, Song C, Hu Y, Han Z, She J, Fan F, Wang J, Jin C, Chang J, Zhou JM, Chai J. Chitin-induced dimerization activates a plant immune receptor. Science. 2012 Jun 1;336(6085):1160-4. PMID:22654057 doi:10.1126/science.1218867

Contents


PDB ID 4ebz

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