8a4o

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8a4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ustilago_hordei Ustilago hordei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A4O FirstGlance]. <br>
<table><tr><td colspan='2'>[[8a4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ustilago_hordei Ustilago hordei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A4O FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8a4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a4o OCA], [https://pdbe.org/8a4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a4o RCSB], [https://www.ebi.ac.uk/pdbsum/8a4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a4o ProSAT]</span></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=8a4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a4o OCA], [https://pdbe.org/8a4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a4o RCSB], [https://www.ebi.ac.uk/pdbsum/8a4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a4o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/I2G262_USTHO I2G262_USTHO]
[https://www.uniprot.org/uniprot/I2G262_USTHO I2G262_USTHO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plant-pathogenic fungi are causative agents of the majority of plant diseases and can lead to severe crop loss in infected populations. Fungal colonization is achieved by combining different strategies, such as avoiding and counteracting the plant immune system and manipulating the host metabolome. Of major importance are virulence factors secreted by fungi, which fulfil diverse functions to support the infection process. Most of these proteins are highly specialized, with structural and biochemical information often absent. Here, we present the atomic structures of the cerato-platanin-like protein Cpl1 from Ustilago maydis and its homologue Uvi2 from Ustilago hordei. Both proteins adopt a double-Psibeta-barrel architecture reminiscent of cerato-platanin proteins, a class so far not described in smut fungi. Our structure-function analysis shows that Cpl1 binds to soluble chitin fragments via two extended grooves at the dimer interface of the two monomer molecules. This carbohydrate-binding mode has not been observed previously and expands the repertoire of chitin-binding proteins. Cpl1 localizes to the cell wall of U. maydis and might synergize with cell wall-degrading and decorating proteins during maize infection. The architecture of Cpl1 harbouring four surface-exposed loop regions supports the idea that it might play a role in the spatial coordination of these proteins. While deletion of cpl1 has only mild effects on the virulence of U. maydis, a recent study showed that deletion of uvi2 strongly impairs U. hordei virulence. Our structural comparison between Cpl1 and Uvi2 reveals sequence variations in the loop regions that might explain a diverging function.
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Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi.,Weiland P, Dempwolff F, Steinchen W, Freibert SA, Tian H, Glatter T, Martin R, Thomma BPHJ, Bange G, Altegoer F Mol Plant Pathol. 2023 Jul;24(7):768-787. doi: 10.1111/mpp.13349. Epub 2023 May , 12. PMID:37171083<ref>PMID:37171083</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8a4o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of the Ustilago hordei effector protein Uvi2

PDB ID 8a4o

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