|Title||The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.|
|Publication Type||Journal Article|
|Year of Publication||1999|
|Authors||Fant, F., W. F. Vranken, and F. A. Borremans|
|Date Published||1999 Nov 15|
|Keywords||Amino Acid Sequence, Defensins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Plant Proteins, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Proteins, Rosales, Sequence Alignment, Solutions|
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.
The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.