8xgl
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8xgl is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Magnaporthe oryzae effector NIS1== | |
| + | <StructureSection load='8xgl' size='340' side='right'caption='[[8xgl]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8xgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae Pyricularia oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XGL 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]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8xgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xgl OCA], [https://pdbe.org/8xgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xgl RCSB], [https://www.ebi.ac.uk/pdbsum/8xgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xgl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NIS1_PYRO7 NIS1_PYRO7] Secreted effector that induces necrotic lesions in Nicotiana benthamiana (PubMed:22352720). Interacts with the rice receptor-like kinases (RLKs) BAK1/SERK3 and BKK1/SERK4, inhibits their kinase activity and suppresses INF1-induced pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) in N.benthamiana (PubMed:30584105). Also interacts with the rice receptor-like cytoplasmic kinase (RLCK) BIK1 and inhibits its kinase activity, thereby inhibiting PAMP-induced ROS generation (PubMed:30584105). In PTI, phosphorylation relaying by RLKs and RLCKs is critical for the initiation of downstream signaling (PubMed:30584105). Suppresses R3a/Avr3a-dependent hypersensitive response (HR) cell death and thus may have additional targets, probably belonging to a kinase family that regulates Avr3a effector-triggered immunity (ETI) (PubMed:30584105).<ref>PMID:22352720</ref> <ref>PMID:30584105</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Necrosis-inducing secreted protein 1 (NIS1) is a core effector of Ascomycota and Basidiomycota fungi. They inhibit the immune responses of host plants mainly through interaction with the multi-functional coreceptor BRI1-associated receptor kinase 1 (BAK1). However, the structural mechanism of the NIS1 family and how they are recognized by BAK1 are unknown. Herein, we report the first crystal structure of the NIS1 family protein, the Magnaporthe oryzae NIS1 (MoNIS1), analyze the recognition mechanism of NIS1s by BAK1, and explore regulation of the NIS1-BAK1 interaction by a chemical compound. MoNIS1 exists as a beta barrel formed by eight beta strands, a folding mode that has not been reported. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) assay suggested that beta4-beta5 loop and beta5 strand of MoNIS1 participate in OsBAK1 interaction, which was supported by further single-point mutational assays. For OsBAK1, HDX-MS assay suggested four regions involved in MoNIS1 interaction. Additionally, we identified a compound that blocks MoNIS1-OsBAK1 interaction in vitro and inhibits the virulence of M. oryzae on rice. Collectively, we determined the first structure of NIS1 family effectors, presented the recognition mechanism of NIS1 by BAK1, and showed that blocking NIS1-BAK1 interaction could be a new target for fungicide development. | ||
| - | + | Understanding and manipulating the recognition of necrosis-inducing secreted protein 1 (NIS1) by BRI1-associated receptor kinase 1 (BAK1).,Han R, Zhu T, Kong Z, Zhang X, Wang D, Liu J Int J Biol Macromol. 2024 Oct;278(Pt 3):134821. doi: , 10.1016/j.ijbiomac.2024.134821. Epub 2024 Aug 16. PMID:39154678<ref>PMID:39154678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8xgl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyricularia oryzae]] | ||
| + | [[Category: Han R]] | ||
| + | [[Category: Liu J]] | ||
| + | [[Category: Wang D]] | ||
| + | [[Category: Zhang X]] | ||
Current revision
Structure of the Magnaporthe oryzae effector NIS1
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Categories: Large Structures | Pyricularia oryzae | Han R | Liu J | Wang D | Zhang X
