View source for 8a14


==Crystal structure of the cerato-platanin-like protein Cpl1 from Ustilago maydis==
<StructureSection load='8a14' size='340' side='right'caption='[[8a14]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8a14]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ustilago_maydis_521 Ustilago maydis 521]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A14 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]] 1.9&#8491;</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=8a14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a14 OCA], [https://pdbe.org/8a14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a14 RCSB], [https://www.ebi.ac.uk/pdbsum/8a14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a14 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0D1E4Q7_USTMA A0A0D1E4Q7_USTMA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8a14" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ustilago maydis 521]]
[[Category: Altegoer F]]
[[Category: Bange G]]
[[Category: Weiland P]]