View source for 7zvh


==Penicillium expansum antifungal protein B==
<StructureSection load='7zvh' size='340' side='right'caption='[[7zvh]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_expansum Penicillium expansum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZVH 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]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7zvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zvh OCA], [https://pdbe.org/7zvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zvh RCSB], [https://www.ebi.ac.uk/pdbsum/7zvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zvh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0A2K0J0_PENEN A0A0A2K0J0_PENEN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antifungal proteins (AFPs) are promising antimicrobial compounds that represent a feasible alternative to fungicides. Penicillium expansum encodes three phylogenetically distinct AFPs (PeAfpA, PeAfpB and PeAfpC) which show different antifungal profiles and fruit protection effects. To gain knowledge about the structural determinants governing their activity, we solved the crystal structure of PeAfpB and rationally designed five PeAfpA::PeAfpB chimeras (chPeAFPV1-V5). Chimeras showed significant differences in their antifungal activity. chPeAFPV1 and chPeAFPV2 improved the parental PeAfpB potency, and it was very similar to that of PeAfpA. chPeAFPV4 and chPeAFPV5 showed an intermediate profile of activity compared to the parental proteins while chPeAFPV3 was inactive towards most of the fungi tested. Structural analysis of the chimeras evidenced an identical scaffold to PeAfpB, suggesting that the differences in activity are due to the contributions of specific residues and not to induced conformational changes or structural rearrangements. Results suggest that mannoproteins determine protein interaction with the cell wall and its antifungal activity while there is not a direct correlation between binding to membrane phospholipids and activity. This work provides new insights about the relevance of sequence motifs and the feasibility of modifying protein specificity, opening the door to the rational design of chimeras with biotechnological applicability.

Rationally designed antifungal protein chimeras reveal new insights into structure-activity relationship.,Giner-Llorca M, Gallego del Sol F, Marcos JF, Marina A, Manzanares P Int J Biol Macromol. 2023 Jan 15;225:135-148. doi: , 10.1016/j.ijbiomac.2022.11.280. Epub 2022 Nov 29. PMID:36460243<ref>PMID:36460243</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zvh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Penicillium expansum]]
[[Category: Gallego del Sol F]]
[[Category: Giner Llorca M]]
[[Category: Manzanares P]]
[[Category: Marcos JF]]
[[Category: Marina A]]