1BK8

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


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 500 
  • Conformers Submitted: 25 
  • Selection Criteria: LEAST RESTRAINT VIOLATION AND ENERGY 

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This is version 1.3 of the entry. See complete history


Literature

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

Fant, F.Vranken, W.F.Borremans, F.A.

(1999) Proteins 37: 388-403

  • DOI: https://doi.org/10.1002/(sici)1097-0134(19991115)37:3<388::aid-prot7>3.3.co;2-6
  • Primary Citation of Related Structures:  
    1BK8

  • 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.


  • Organizational Affiliation

    Department of Organic Chemistry, University of Gent, Belgium. franky.fant@rug.ac.be


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ANTIMICROBIAL PROTEIN 150Aesculus hippocastanumMutation(s): 0 
UniProt
Find proteins for Q7M1F3 (Aesculus hippocastanum)
Explore Q7M1F3 
Go to UniProtKB:  Q7M1F3
Entity Groups  
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UniProt GroupQ7M1F3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 500 
  • Conformers Submitted: 25 
  • Selection Criteria: LEAST RESTRAINT VIOLATION AND ENERGY 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-01-05
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other