2lb7

Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif

spinqualitylabelsall models 2lb7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lb7 is a 1 chain structure with sequence from Triticum kiharae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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