4b9h

From Proteopedia

(Difference between revisions)

Current revision

Cladosporium fulvum LysM effector Ecp6 in complex with a beta-1,4- linked N-acetyl-D-glucosamine tetramer: I3C heavy atom derivative

Structural highlights

4b9h is a 1 chain structure with sequence from Fulvia fulva. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSM_PASFU Secreted effector that enables the plant pathogenic fungus to manipulate host defenses for successful infection (PubMed:18452583). Binds chitine, but not to any other glycan, including the N-linked glycan chitobiose (PubMed:20724636). Outcompetes host immune receptor for chitin binding through intrachain LysM dimerization (PubMed:18452583, PubMed:20724636). During infection, sequesters chitin oligosaccharides that are released from the cell walls of invading hyphae to prevent elicitation of host immunity (PubMed:20724636).^[1] ^[2]

Publication Abstract from PubMed

While host immune receptors detect pathogen-associated molecular patterns to activate immunity, pathogens attempt to deregulate host immunity through secreted effectors. Fungi employ LysM effectors to prevent recognition of cell wall-derived chitin by host immune receptors, although the mechanism to compete for chitin binding remained unclear. Structural analysis of the LysM effector Ecp6 of the fungal tomato pathogen Cladosporium fulvum reveals a novel mechanism for chitin binding, mediated by intrachain LysM dimerization, leading to a chitin-binding groove that is deeply buried in the effector protein. This composite binding site involves two of the three LysMs of Ecp6 and mediates chitin binding with ultra-high (pM) affinity. Intriguingly, the remaining singular LysM domain of Ecp6 binds chitin with low micromolar affinity but can nevertheless still perturb chitin-triggered immunity. Conceivably, the perturbation by this LysM domain is not established through chitin sequestration but possibly through interference with the host immune receptor complex. DOI:http://dx.doi.org/10.7554/eLife.00790.001.

Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization.,Sanchez-Vallet A, Saleem-Batcha R, Kombrink A, Hansen G, Valkenburg DJ, Thomma BP, Mesters JR Elife. 2013 Jul 2;2:e00790. doi: 10.7554/eLife.00790. Print 2013. PMID:23840930^[3]

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

References

↑ Bolton MD, van Esse HP, Vossen JH, de Jonge R, Stergiopoulos I, Stulemeijer IJ, van den Berg GC, Borrás-Hidalgo O, Dekker HL, de Koster CG, de Wit PJ, Joosten MH, Thomma BP. The novel Cladosporium fulvum lysin motif effector Ecp6 is a virulence factor with orthologues in other fungal species. Mol Microbiol. 2008 Jul;69(1):119-36. PMID:18452583 doi:10.1111/j.1365-2958.2008.06270.x
↑ de Jonge R, van Esse HP, Kombrink A, Shinya T, Desaki Y, Bours R, van der Krol S, Shibuya N, Joosten MH, Thomma BP. Conserved fungal LysM effector Ecp6 prevents chitin-triggered immunity in plants. Science. 2010 Aug 20;329(5994):953-5. PMID:20724636 doi:10.1126/science.1190859
↑ Sanchez-Vallet A, Saleem-Batcha R, Kombrink A, Hansen G, Valkenburg DJ, Thomma BP, Mesters JR. Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization. Elife. 2013 Jul 2;2:e00790. doi: 10.7554/eLife.00790. Print 2013. PMID:23840930 doi:10.7554/eLife.00790

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/4b9h"

@@ Line 3: / Line 3: @@
 <StructureSection load='4b9h' size='340' side='right'caption='[[4b9h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4b9h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4b9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fulvia_fulva Fulvia fulva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3C:5-AMINO-2,4,6-TRIIODOBENZENE-1,3-DICARBOXYLIC+ACID'>I3C</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b8v|4b8v]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3C:5-AMINO-2,4,6-TRIIODOBENZENE-1,3-DICARBOXYLIC+ACID'>I3C</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=4b9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9h OCA], [https://pdbe.org/4b9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9h RCSB], [https://www.ebi.ac.uk/pdbsum/4b9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9h ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/LYSM_PASFU LYSM_PASFU] Secreted effector that enables the plant pathogenic fungus to manipulate host defenses for successful infection (PubMed:18452583). Binds chitine, but not to any other glycan, including the N-linked glycan chitobiose (PubMed:20724636). Outcompetes host immune receptor for chitin binding through intrachain LysM dimerization (PubMed:18452583, PubMed:20724636). During infection, sequesters chitin oligosaccharides that are released from the cell walls of invading hyphae to prevent elicitation of host immunity (PubMed:20724636).<ref>PMID:18452583</ref> <ref>PMID:20724636</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Fulvia fulva]]
 [[Category: Large Structures]]
-[[Category: Hansen, G]]
+[[Category: Hansen G]]
-[[Category: Mesters, J R]]
+[[Category: Mesters JR]]
-[[Category: Saleem-Batcha, R]]
+[[Category: Saleem-Batcha R]]
-[[Category: Sanchez-Vallet, A]]
+[[Category: Sanchez-Vallet A]]
-[[Category: Thomma, B P.H J]]
+[[Category: Thomma BPHJ]]
-[[Category: Sugar binding protein]]

4b9h

From Proteopedia

Current revision

Cladosporium fulvum LysM effector Ecp6 in complex with a beta-1,4- linked N-acetyl-D-glucosamine tetramer: I3C heavy atom derivative

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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