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PDBsum entry 1bk8
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Plant defensin
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PDB id
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1bk8
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References listed in PDB file
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Key reference
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Title
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The three-Dimensional solution structure of aesculus hippocastanum antimicrobial protein 1 determined by 1h nuclear magnetic resonance.
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Authors
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F.Fant,
W.F.Vranken,
F.A.Borremans.
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Ref.
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Proteins, 1999,
37,
388-403.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 5.
Figure 5. Polypeptide backbone of the Gln8-Asn16 fragment and
the side chain of Trp10 of Ah-AMP1.
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Figure 7.
Figure 7. Schematic representation of the N- and C-termini and
the disulfide bond connecting them for Ah-AMP1 (red) and Rs-AFP1
(green). The free electron pairs of the cysteine sulfur atoms
are shown only for Rs-AFP1.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(1999,
37,
388-403)
copyright 1999.
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