The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.
Aesculus hippocastanum antimicrobial protein 1 (Ah-AMP1) is a plant defensin isolated from horse chestnuts. The plant defensins have been divided in several subfamilies according to their amino acid sequence homology. Ah-AMP1, belonging to subfamily A2, inhibits growth of a broad range of fungi. So far, a three-dimensional structure has been determined only for members of subfamilies A3 and B2. In order to understand activity and specificity of these plant defensins, the structure of a protein belonging to subfamily A2 is needed. We report the three-dimensional solution structure of Ah-AMP1 as determined from two-dimensional 1H nuclear magnetic resonance data. The structure features all the characteristics of the "cysteine-stabilized alpha beta-motif." A comparison of the structure, the electrostatic potential surface and regions important for interaction with the fungal receptor, is made with Rs-AFP1 (plant defensin of subfamily A3). Thus, residues important for activity and specificity have been assigned.
Fant
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Department of Organic Chemistry, University of Gent, Belgium. franky.fant@rug.ac.be
Vranken
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Borremans
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D000595:Amino Acid Sequence; D023082:Defensins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D019685:Rosales / Q000737:chemistry*; D016415:Sequence Alignment; D012996:Solutions
C404483:Ah-AMP1protein, Aesculus hippocastanum; D023082:Defensins; D010940:Plant Proteins; D011506:Proteins; D012996:Solutions