5jcd

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of OsCEBiP

Structural highlights

5jcd is a 3 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 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CEBIP_ORYSJ Chitin elicitor-binding protein involved in the perception and transduction of chitin oligosaccharide elicitor signal for defense responses.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Chitin is the major component of fungal cell wall and serves as a molecular pattern that can be recognized by the receptor OsCEBiP in rice, a lysine motif (LysM) receptor-like protein (RLP), to trigger immune responses. The molecular mechanisms underlying chitin recognition remain elusive. Here we report the crystal structures of the ectodomain of OsCEBiP (OsCEBiP-ECD) in free and chitin-bound forms. The structures reveal that OsCEBiP-ECD contains three tandem LysMs followed by a novel structure fold of cysteine-rich domain. The structures showed that chitin binding induces no striking conformational changes in OsCEBiP. Structural comparison among N-acetylglucosamine (NAG) oligomer-bound LysMs revealed a highly conserved recognition mechanism, which is expected to facilitate study of other LysM-containing proteins for their NAG binding. Modeling study showed that chitin induces OsCEBiP homodimerization in a "sliding mode". Our data provide insights into rice chitin receptor-mediated immunity triggered by fungal cell wall.

Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP.,Liu S, Wang J, Han Z, Gong X, Zhang H, Chai J Structure. 2016 May 24. pii: S0969-2126(16)30075-2. doi:, 10.1016/j.str.2016.04.014. PMID:27238968^[4]

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

References

↑ Kaku H, Nishizawa Y, Ishii-Minami N, Akimoto-Tomiyama C, Dohmae N, Takio K, Minami E, Shibuya N. Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc Natl Acad Sci U S A. 2006 Jul 18;103(29):11086-91. Epub 2006 Jul 7. PMID:16829581 doi:http://dx.doi.org/0508882103
↑ 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
↑ Liu S, Wang J, Han Z, Gong X, Zhang H, Chai J. Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP. Structure. 2016 May 24. pii: S0969-2126(16)30075-2. doi:, 10.1016/j.str.2016.04.014. PMID:27238968 doi:http://dx.doi.org/10.1016/j.str.2016.04.014

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/5jcd"

Categories: Large Structures | Oryza sativa Japonica Group | Chai JJ | Liu SM | Wang JZ

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5jcd is ON HOLD
+==Crystal structure of OsCEBiP==
+<StructureSection load='5jcd' size='340' side='right'caption='[[5jcd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5jcd]] is a 3 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=5JCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5jcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jcd OCA], [https://pdbe.org/5jcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jcd RCSB], [https://www.ebi.ac.uk/pdbsum/5jcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jcd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CEBIP_ORYSJ CEBIP_ORYSJ] Chitin elicitor-binding protein involved in the perception and transduction of chitin oligosaccharide elicitor signal for defense responses.<ref>PMID:16829581</ref> <ref>PMID:21070404</ref> <ref>PMID:22891159</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Chitin is the major component of fungal cell wall and serves as a molecular pattern that can be recognized by the receptor OsCEBiP in rice, a lysine motif (LysM) receptor-like protein (RLP), to trigger immune responses. The molecular mechanisms underlying chitin recognition remain elusive. Here we report the crystal structures of the ectodomain of OsCEBiP (OsCEBiP-ECD) in free and chitin-bound forms. The structures reveal that OsCEBiP-ECD contains three tandem LysMs followed by a novel structure fold of cysteine-rich domain. The structures showed that chitin binding induces no striking conformational changes in OsCEBiP. Structural comparison among N-acetylglucosamine (NAG) oligomer-bound LysMs revealed a highly conserved recognition mechanism, which is expected to facilitate study of other LysM-containing proteins for their NAG binding. Modeling study showed that chitin induces OsCEBiP homodimerization in a "sliding mode". Our data provide insights into rice chitin receptor-mediated immunity triggered by fungal cell wall.
-Authors: Chai, J.J., Liu, S.M., Wang, J.Z.
+Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP.,Liu S, Wang J, Han Z, Gong X, Zhang H, Chai J Structure. 2016 May 24. pii: S0969-2126(16)30075-2. doi:, 10.1016/j.str.2016.04.014. PMID:27238968<ref>PMID:27238968</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wang, J.Z]]
+<div class="pdbe-citations 5jcd" style="background-color:#fffaf0;"></div>
-[[Category: Chai, J.J]]
+== References ==
-[[Category: Liu, S.M]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Oryza sativa Japonica Group]]
+[[Category: Chai JJ]]
+[[Category: Liu SM]]
+[[Category: Wang JZ]]

5jcd

From Proteopedia

Current revision

Crystal structure of OsCEBiP

Structural highlights

Function

Publication Abstract from PubMed

References

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