7nmm
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Complex of rice blast (Magnaporthe oryzae) effector protein APikL2F with the host target sHMA94 from Setaria italica== |
| - | <StructureSection load='7nmm' size='340' side='right'caption='[[7nmm]]' scene=''> | + | <StructureSection load='7nmm' size='340' side='right'caption='[[7nmm]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7nmm]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae_B157 Pyricularia oryzae B157] and [https://en.wikipedia.org/wiki/Setaria_italica Setaria italica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NMM FirstGlance]. <br> |
| - | </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=7nmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nmm OCA], [https://pdbe.org/7nmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nmm RCSB], [https://www.ebi.ac.uk/pdbsum/7nmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nmm ProSAT]</span></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]] 2.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7nmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nmm OCA], [https://pdbe.org/7nmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nmm RCSB], [https://www.ebi.ac.uk/pdbsum/7nmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nmm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K3YDQ6_SETIT K3YDQ6_SETIT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Accelerated gene evolution is a hallmark of pathogen adaptation and specialization following host-jumps. However, the molecular processes associated with adaptive evolution between host-specific lineages of a multihost plant pathogen remain poorly understood. In the blast fungus Magnaporthe oryzae (Syn. Pyricularia oryzae), host specialization on different grass hosts is generally associated with dynamic patterns of gain and loss of virulence effector genes that tend to define the distinct genetic lineages of this pathogen. Here, we unravelled the biochemical and structural basis of adaptive evolution of APikL2, an exceptionally conserved paralog of the well-studied rice-lineage specific effector AVR-Pik. Whereas AVR-Pik and other members of the six-gene AVR-Pik family show specific patterns of presence/absence polymorphisms between grass-specific lineages of M. oryzae, APikL2 stands out by being ubiquitously present in all blast fungus lineages from 13 different host species. Using biochemical, biophysical and structural biology methods, we show that a single aspartate to asparagine polymorphism expands the binding spectrum of APikL2 to host proteins of the heavy-metal associated (HMA) domain family. This mutation maps to one of the APikL2-HMA binding interfaces and contributes to an altered hydrogen-bonding network. By combining phylogenetic ancestral reconstruction with an analysis of the structural consequences of allelic diversification, we revealed a common mechanism of effector specialization in the AVR-Pik/APikL2 family that involves two major HMA-binding interfaces. Together, our findings provide a detailed molecular evolution and structural biology framework for diversification and adaptation of a fungal pathogen effector family following host-jumps. | ||
| + | |||
| + | A single amino acid polymorphism in a conserved effector of the multihost blast fungus pathogen expands host-target binding spectrum.,Bentham AR, Petit-Houdenot Y, Win J, Chuma I, Terauchi R, Banfield MJ, Kamoun S, Langner T PLoS Pathog. 2021 Nov 10;17(11):e1009957. doi: 10.1371/journal.ppat.1009957. , eCollection 2021 Nov. PMID:34758051<ref>PMID:34758051</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7nmm" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Avirulence protein 3D structures|Avirulence protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Pyricularia oryzae B157]] |
| + | [[Category: Setaria italica]] | ||
| + | [[Category: Banfield MJ]] | ||
| + | [[Category: Bentham AR]] | ||
Revision as of 12:36, 1 February 2024
Complex of rice blast (Magnaporthe oryzae) effector protein APikL2F with the host target sHMA94 from Setaria italica
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