1BK8

DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF AESCULUS HIPPOCASTANUM ANTIMICROBIAL PROTEIN 1 (AH-AMP1) BY 1H NMR, 25 STRUCTURES

Summary for 1BK8

• Entry DOI: 10.2210/pdb1bk8/pdb
• Descriptor: ANTIMICROBIAL PROTEIN 1 (1 entity in total)
• Functional Keywords: plant defensin, antimicrobial, cysteine-stabilized alfa/ beta motif
• Biological source: Aesculus hippocastanum (common horse chestnut)
• Cellular location: Secreted : Q7M1F3
• Total number of polymer chains: 1
• Total formula weight: 5873.52

Authors

Fant, F.,Borremans, F.A.M. (deposition date: 1998-07-15, release date: 2000-01-05, Last modification date: 2024-10-30)

Primary citation

Fant, F.,Vranken, W.F.,Borremans, F.A.
The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.
Proteins, 37:388-403, 1999

PubMed 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.

PubMed: 10591099
DOI: 10.1002/(SICI)1097-0134(19991115)37:3<388::AID-PROT7>3.3.CO;2-6

Experimental method

SOLUTION NMR