1p9z
From Proteopedia
(New page: 200px<br /><applet load="1p9z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9z" /> '''The Solution Structure of Antifungal Peptide...) |
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'''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver'''<br /> | '''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure in aqueous solution of Eucommia antifungal | + | The three-dimensional structure in aqueous solution of Eucommia antifungal peptide 2 (EAFP2) from Eucommia ulmoides Oliv was determined using (1)H NMR spectroscopy. EAFP2 is a newly discovered 41-residue peptide distinct with a five-disulfide cross-linked motif. This peptide exhibits chitin-binding activity and inhibitory effects on the growth of cell wall chitin-containing fungi and chitin-free fungi. The structure was calculated by using torsion angle dynamic simulated annealing with a total of 614 distance restraints and 16 dihedral restraints derived from NOESY and DQF-COSY spectra, respectively. The five disulfide bonds were assigned from preliminary structures using a statistical analysis of intercystinyl distances. The solution structure of EAFP2 is presented as an ensemble of 20 conformers with a backbone RMS deviation of 0.65 (+/-0.13) A for the well-defined Cys3-Cys39 segment. The tertiary structure of EAFP2 represents the first five-disulfide cross-linked structural model of the plant antifungal peptide. EAFP2 adopts a compact global fold composed of a 3(10) helix (Cys3-Arg6), an alpha-helix (Gly26-Cys30), and a three-strand antiparallel beta-sheet (Cys16-Ser18, Tyr22-Gly24, and Arg36-Cys37). The tertiary structure of EAFP2 shows a chitin-binding domain (residues 11-30) with a hydrophobic face and a characteristic sector formed by the N-terminal 10 residues and the C-terminal segment cross-linked through the unique disulfide bond Cys7-Cys37, which brings all four positively charged residues (Arg6, Arg9, Arg36, and Arg40) onto a cationic face. On the basis of such a structural feature, the possible structural basis for the functional properties of EAFP2 is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1P9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eucommia_ulmoides Eucommia ulmoides]. Full crystallographic information is available from [http:// | + | 1P9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eucommia_ulmoides Eucommia ulmoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Eucommia ulmoides]] | [[Category: Eucommia ulmoides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Huang, R | + | [[Category: Huang, R H.]] |
| - | [[Category: Tu, G | + | [[Category: Tu, G Z.]] |
| - | [[Category: Wang, D | + | [[Category: Wang, D C.]] |
[[Category: Xiang, Y.]] | [[Category: Xiang, Y.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
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[[Category: disulfide stabilized motif]] | [[Category: disulfide stabilized motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:43 2008'' |
Revision as of 12:26, 21 February 2008
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The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver
Overview
The three-dimensional structure in aqueous solution of Eucommia antifungal peptide 2 (EAFP2) from Eucommia ulmoides Oliv was determined using (1)H NMR spectroscopy. EAFP2 is a newly discovered 41-residue peptide distinct with a five-disulfide cross-linked motif. This peptide exhibits chitin-binding activity and inhibitory effects on the growth of cell wall chitin-containing fungi and chitin-free fungi. The structure was calculated by using torsion angle dynamic simulated annealing with a total of 614 distance restraints and 16 dihedral restraints derived from NOESY and DQF-COSY spectra, respectively. The five disulfide bonds were assigned from preliminary structures using a statistical analysis of intercystinyl distances. The solution structure of EAFP2 is presented as an ensemble of 20 conformers with a backbone RMS deviation of 0.65 (+/-0.13) A for the well-defined Cys3-Cys39 segment. The tertiary structure of EAFP2 represents the first five-disulfide cross-linked structural model of the plant antifungal peptide. EAFP2 adopts a compact global fold composed of a 3(10) helix (Cys3-Arg6), an alpha-helix (Gly26-Cys30), and a three-strand antiparallel beta-sheet (Cys16-Ser18, Tyr22-Gly24, and Arg36-Cys37). The tertiary structure of EAFP2 shows a chitin-binding domain (residues 11-30) with a hydrophobic face and a characteristic sector formed by the N-terminal 10 residues and the C-terminal segment cross-linked through the unique disulfide bond Cys7-Cys37, which brings all four positively charged residues (Arg6, Arg9, Arg36, and Arg40) onto a cationic face. On the basis of such a structural feature, the possible structural basis for the functional properties of EAFP2 is discussed.
About this Structure
1P9Z is a Single protein structure of sequence from Eucommia ulmoides. Full crystallographic information is available from OCA.
Reference
Solution structure of Eucommia antifungal peptide: a novel structural model distinct with a five-disulfide motif., Huang RH, Xiang Y, Tu GZ, Zhang Y, Wang DC, Biochemistry. 2004 May 25;43(20):6005-12. PMID:15147184
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