1AYJ
DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF RAPHANUS SATIVUS ANTIFUNGAL PROTEIN 1 (RS-AFP1) BY 1H NMR, 20 STRUCTURES
Summary for 1AYJ
| Entry DOI | 10.2210/pdb1ayj/pdb |
| Descriptor | ANTIFUNGAL PROTEIN 1 (1 entity in total) |
| Functional Keywords | fungicide, plant defensin, cysteine-stabilized alfa/beta motif |
| Biological source | Raphanus sativus var. niger (Chinese radish) |
| Total number of polymer chains | 1 |
| Total formula weight | 5685.55 |
| Authors | Fant, F.,Borremans, F.A.M. (deposition date: 1997-11-05, release date: 1998-01-28, Last modification date: 2024-10-23) |
| Primary citation | Fant, F.,Vranken, W.,Broekaert, W.,Borremans, F. Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR. J.Mol.Biol., 279:257-270, 1998 Cited by PubMed Abstract: Raphanus sativus Antifungal Protein 1 (Rs-AFP1) is a 51 amino acid residue plant defensin isolated from radish (Raphanus sativus L.) seeds. The three-dimensional structure in aqueous solution has been determined from two-dimensional 1H NMR data recorded at 500 MHz using the DIANA/REDAC calculation protocols. Experimental constraints consisted of 787 interproton distances extracted from NOE cross-peaks, 89 torsional constraints from 106 vicinal interproton coupling constants and 32 stereospecific assignments of prochiral protons. Further refinement by simulated annealing resulted in a set of 20 structures having pairwise root-mean-square differences of 1.35(+/- 0.35) A over the backbone heavy atoms and 2.11(+/- 0.46) A over all heavy atoms. The molecule adopts a compact globular fold comprising an alpha-helix from Asn18 till Leu28 and a triple-stranded beta-sheet (beta 1 = Lys2-Arg6, beta 2 = His33-Tyr38 and beta 3 = His43-Pro50). The central strand of this beta-sheet is connected by two disulfide bridges (Cys21-Cys45 and Cys25-Cys47) to the alpha-helix. The connection between beta-strand 2 and 3 is formed by a type VIa beta-turn. Even the loop (Pro7 to Asn17) between beta-strand 1 and the alpha-helix is relatively well defined. The structure of Raphanus sativus Antifungal Protein 1 features all the characteristics of the "cysteine stabilized alpha beta motif". A comparison of the complete structure and of the regions important for interaction with the fungal receptor according to a mutational study, is made with the structure of gamma-thionin, a plant defensin that has no antifungal activity. It is concluded that this interaction is both electrostatic and specific, and some possible scenarios for the mode of action are given. PubMed: 9636715DOI: 10.1006/jmbi.1998.1767 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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