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| | ==Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif== | | ==Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif== |
| - | <StructureSection load='2lb7' size='340' side='right'caption='[[2lb7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lb7' size='340' side='right'caption='[[2lb7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lb7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trikh Trikh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lb7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_kiharae Triticum kiharae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LB7 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=2lb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lb7 OCA], [https://pdbe.org/2lb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lb7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lb7 ProSAT]</span></td></tr> | | </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=2lb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lb7 OCA], [https://pdbe.org/2lb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lb7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lb7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AMP_TRIKH AMP_TRIKH]] Binds chitin. WAMP-1a has antifungal activity against the fungi F.solani (IC(50)=5 ug/ml), F.verticillioides (IC(50)=30 ug/ml), F.oxysporum (IC(50)=5 ug/ml), B.sorokiniana (IC(50)=5 ug/ml), B.cinerea (IC(50)=20 ug/ml) and N.crassa (IC(50)=10 ug/ml). Inhibits hyphal elongation and causes browning of hyphae in F.oxysporum. Causes destruction and discoloration of spores in B.sorokiniana. Inhibits the development of disease caused by the fungus P.infestans on potato tubers. Has antibacterial activity against the Gram-negative bacteria P.syringae and E.carotovora, and the Gram-positive bacterium C.michiganensis.<ref>PMID:19583772</ref>
| + | [https://www.uniprot.org/uniprot/AMP_TRIKH AMP_TRIKH] Binds chitin. WAMP-1a has antifungal activity against the fungi F.solani (IC(50)=5 ug/ml), F.verticillioides (IC(50)=30 ug/ml), F.oxysporum (IC(50)=5 ug/ml), B.sorokiniana (IC(50)=5 ug/ml), B.cinerea (IC(50)=20 ug/ml) and N.crassa (IC(50)=10 ug/ml). Inhibits hyphal elongation and causes browning of hyphae in F.oxysporum. Causes destruction and discoloration of spores in B.sorokiniana. Inhibits the development of disease caused by the fungus P.infestans on potato tubers. Has antibacterial activity against the Gram-negative bacteria P.syringae and E.carotovora, and the Gram-positive bacterium C.michiganensis.<ref>PMID:19583772</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trikh]] | + | [[Category: Triticum kiharae]] |
| - | [[Category: Arseniev, A S]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Balashova, T A]] | + | [[Category: Balashova TA]] |
| - | [[Category: Egorov, T A]] | + | [[Category: Egorov TA]] |
| - | [[Category: Grishin, E V]] | + | [[Category: Grishin EV]] |
| - | [[Category: Odintsova, T I]] | + | [[Category: Odintsova TI]] |
| - | [[Category: Vassilevski, A A]] | + | [[Category: Vassilevski AA]] |
| - | [[Category: Antimicrobial protein]]
| + | |
| Structural highlights
Function
AMP_TRIKH Binds chitin. WAMP-1a has antifungal activity against the fungi F.solani (IC(50)=5 ug/ml), F.verticillioides (IC(50)=30 ug/ml), F.oxysporum (IC(50)=5 ug/ml), B.sorokiniana (IC(50)=5 ug/ml), B.cinerea (IC(50)=20 ug/ml) and N.crassa (IC(50)=10 ug/ml). Inhibits hyphal elongation and causes browning of hyphae in F.oxysporum. Causes destruction and discoloration of spores in B.sorokiniana. Inhibits the development of disease caused by the fungus P.infestans on potato tubers. Has antibacterial activity against the Gram-negative bacteria P.syringae and E.carotovora, and the Gram-positive bacterium C.michiganensis.[1]
Publication Abstract from PubMed
Hevein, a well-studied lectin from the rubber tree Hevea brasiliensis, is the title representative of a broad family of chitin-binding polypeptides. WAMP-1a, a peptide isolated from the wheat Triticum kiharae, shares considerable similarity with hevein. The peptide possesses antifungal, antibacterial activity and is thought to play an important role in the defense system of wheat. Importantly, it features a substitution of the conserved serine residue to glycine reducing its carbohydrate-binding capacity. We used NMR spectroscopy to derive the spatial structure of WAMP-1a in aqueous solution. Notably, the mutation was found to strengthen amphiphilicity of the molecule, associated with its mode of action, an indication of the hevein domain multi-functionality. Both primary and tertiary structure of WAMP-1a suggest its evolutionary origin from the hevein domain of plant chitinases.
Solution structure of a defense peptide from wheat with a 10-cysteine motif.,Dubovskii PV, Vassilevski AA, Slavokhotova AA, Odintsova TI, Grishin EV, Egorov TA, Arseniev AS Biochem Biophys Res Commun. 2011 Jul 22;411(1):14-8. Epub 2011 Jun 14. PMID:21704019[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif. FEBS J. 2009 Aug;276(15):4266-75. Epub 2009 Jul 3. PMID:19583772 doi:10.1111/j.1742-4658.2009.07135.x
- ↑ Dubovskii PV, Vassilevski AA, Slavokhotova AA, Odintsova TI, Grishin EV, Egorov TA, Arseniev AS. Solution structure of a defense peptide from wheat with a 10-cysteine motif. Biochem Biophys Res Commun. 2011 Jul 22;411(1):14-8. Epub 2011 Jun 14. PMID:21704019 doi:10.1016/j.bbrc.2011.06.058
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