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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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From structure:
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ArShift- Aromatic
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Proshift
PPM
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Unread 11-17-2010, 11:06 PM
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Default Determination of the three-dimensional solution structure of Raphanus sativus antifun

Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR.

Related Articles Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR.

J Mol Biol. 1998 May 29;279(1):257-70

Authors: Fant F, Vranken W, Broekaert W, Borremans F

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.

PMID: 9636715 [PubMed - indexed for MEDLINE]



Source: PubMed
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