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7vs7

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Crystal structure of the ectodomain of OsCERK1 in complex with chitin hexamer

Structural highlights

7vs7 is a 1 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.015Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CERK1_ORYSJ Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP) (PubMed:21070404, PubMed:22891159, PubMed:24964058). Involved in the detection of microbial peptidoglycans (PGNs) and mediates PGN response (PubMed:24964058). Plays dual roles in PGN and chitin signaling during innate immunity. Acts as an adapter for LYP4 and LYP6 and mediates signal transduction from the extracellular to intracellular spaces. Participates in the activation of defense genes during response to PGN and chitin (PubMed:25335639). Phosphorylates the downstream partner RLCK185 in response to chitin elicitation (PubMed:23498959).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Plants have developed innate immune systems to fight against pathogenic fungi by monitoring pathogenic signals known as pathogen-associated molecular patterns (PAMP) and have established endo symbiosis with arbuscular mycorrhizal (AM) fungi through recognition of mycorrhizal (Myc) factors. Chitin elicitor receptor kinase 1 of Oryza sativa subsp. Japonica (OsCERK1) plays a bifunctional role in mediating both chitin-triggered immunity and symbiotic relationships with AM fungi. However, it remains unclear whether OsCERK1 can directly recognize chitin molecules. In this study, we show that OsCERK1 binds to the chitin hexamer ((NAG)6 ) and tetramer ((NAG)4 ) directly and determine the crystal structure of the OsCERK1-(NAG)6 complex at 2 A. The structure shows that one OsCERK1 is associated with one (NAG)6 . Upon recognition, chitin hexamer binds OsCERK1 by interacting with the shallow groove on the surface of LysM2. These structural findings, complemented by mutational analyses, demonstrate that LysM2 is crucial for recognition of both (NAG)6 and (NAG)4 . Altogether, these findings provide structural insights into the ability of OsCERK1 in chitin perception, which will lead to a better understanding of the role of OsCERK1 in mediating both immunity and symbiosis in rice.

Structural insight into chitin perception by chitin elicitor receptor kinase 1 of Oryza sativa.,Xu L, Wang J, Xiao Y, Han Z, Chai J J Integr Plant Biol. 2022 May 14. doi: 10.1111/jipb.13279. PMID:35568972^[6]

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

References

↑ Shimizu T, Nakano T, Takamizawa D, Desaki Y, Ishii-Minami N, Nishizawa Y, Minami E, Okada K, Yamane H, Kaku H, Shibuya N. Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. Plant J. 2010 Oct;64(2):204-14. doi: 10.1111/j.1365-313X.2010.04324.x. Epub 2010 , Sep 7. PMID:21070404 doi:http://dx.doi.org/10.1111/j.1365-313X.2010.04324.x
↑ 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
↑ Yamaguchi K, Yamada K, Ishikawa K, Yoshimura S, Hayashi N, Uchihashi K, Ishihama N, Kishi-Kaboshi M, Takahashi A, Tsuge S, Ochiai H, Tada Y, Shimamoto K, Yoshioka H, Kawasaki T. A receptor-like cytoplasmic kinase targeted by a plant pathogen effector is directly phosphorylated by the chitin receptor and mediates rice immunity. Cell Host Microbe. 2013 Mar 13;13(3):347-57. doi: 10.1016/j.chom.2013.02.007. PMID:23498959 doi:http://dx.doi.org/10.1016/j.chom.2013.02.007
↑ Kouzai Y, Mochizuki S, Nakajima K, Desaki Y, Hayafune M, Miyazaki H, Yokotani N, Ozawa K, Minami E, Kaku H, Shibuya N, Nishizawa Y. Targeted gene disruption of OsCERK1 reveals its indispensable role in chitin perception and involvement in the peptidoglycan response and immunity in rice. Mol Plant Microbe Interact. 2014 Sep;27(9):975-82. doi:, 10.1094/MPMI-03-14-0068-R. PMID:24964058 doi:http://dx.doi.org/10.1094/MPMI-03-14-0068-R
↑ Ao Y, Li Z, Feng D, Xiong F, Liu J, Li JF, Wang M, Wang J, Liu B, Wang HB. OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin signaling in rice innate immunity. Plant J. 2014 Dec;80(6):1072-84. doi: 10.1111/tpj.12710. PMID:25335639 doi:http://dx.doi.org/10.1111/tpj.12710
↑ Xu L, Wang J, Xiao Y, Han Z, Chai J. Structural insight into chitin perception by chitin elicitor receptor kinase 1 of Oryza sativa. J Integr Plant Biol. 2022 May 14. doi: 10.1111/jipb.13279. PMID:35568972 doi:http://dx.doi.org/10.1111/jipb.13279

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/7vs7"

Categories: Large Structures | Oryza sativa Japonica Group | Li X

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7vs7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VS7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.015&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vs7 OCA], [https://pdbe.org/7vs7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vs7 RCSB], [https://www.ebi.ac.uk/pdbsum/7vs7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vs7 ProSAT]</span></td></tr>
 </table>

7vs7

From Proteopedia

Current revision

Crystal structure of the ectodomain of OsCERK1 in complex with chitin hexamer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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