Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution.
Crystal 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.
Johnson
Kenneth A
KA
Department of Chemistry, University of Texas at El Paso, 79968, USA.
Kim
Eunsung
E
Teeter
Martha M
MM
Suh
Se Won
SW
Stec
Boguslaw
B
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D001557:Benzenesulfonates; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D001467:Hordeum / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism; D020836:Protein Structure, Quaternary; D012639:Seeds / Q000737:chemistry; D016415:Sequence Alignment; D012694:Serine / Q000737:chemistry / Q000378:metabolism; D014105:Tosyl Compounds / Q000378:metabolism
D023181:Antimicrobial Cationic Peptides; D001557:Benzenesulfonates; D010940:Plant Proteins; D014105:Tosyl Compounds; C036092:hordothionin protein, Hordeum vulgare; D012694:Serine; C029501:4-toluenesulfonic acid