The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.

TitleThe three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.
Publication TypeJournal Article
Year of Publication1999
AuthorsFant, F., W. F. Vranken, and F. A. Borremans
JournalProteins
Volume37
Issue3
Pagination388-403
Date Published1999 Nov 15
ISSN0887-3585
KeywordsAmino 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
Abstract

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.

Alternate JournalProteins
PubMed ID10591099
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