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Crystal Structure of beta hordothioninCrystal Structure of beta hordothionin
Structural highlights
FunctionTHNB_HORVU Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal structure of ubiquitous toxin from barley alpha-hordothionin (alpha-HT) has been determined at 1.9A resolution by X-ray crystallography. The primary sequence as well as the NMR solution structure of alpha-HT firmly established that alpha-HT belongs to a family of membrane active plant toxins-thionins. Since alpha-HT crystallized in a space group (P4(1)2(1)2) that is different from the space group (I422) of previously determined alpha(1)- and beta-purothionins, and visocotoxin A3, therefore, it provided independent information on protein-protein interactions that may be relevant to the toxin mechanism. The structure of alpha-HT not only confirms overall architectural features (crambin fold) but also provides an additional confirmation of the role for crucial solute molecules, that were postulated to be directly involved in the mechanism of toxicity for thionins. Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution.,Johnson KA, Kim E, Teeter MM, Suh SW, Stec B FEBS Lett. 2005 Apr 25;579(11):2301-6. PMID:15848162[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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