1p9z: Difference between revisions

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[[Image:1p9z.gif|left|200px]]<br /><applet load="1p9z" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1p9z.gif|left|200px]]<br /><applet load="1p9z" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1p9z" />

'''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1P9Z OCA].

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==

Line 13:

[[Category: Eucommia ulmoides]]

[[Category: Single protein]]

[[Category: Huang, R.H.]]

[[Category: Huang, R H.]]

[[Category: Tu, G.Z.]]

[[Category: Tu, G Z.]]

[[Category: Wang, D.C.]]

[[Category: Wang, D C.]]

[[Category: Xiang, Y.]]

[[Category: Zhang, Y.]]

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[[Category: disulfide stabilized motif]]

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@@ Line 1: / Line 1: @@
-[[Image:1p9z.gif|left|200px]]<br /><applet load="1p9z" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1p9z.gif|left|200px]]<br /><applet load="1p9z" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1p9z" />
 '''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver'''<br />
 ==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.
+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==
-P9Z 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9Z OCA].
+P9Z 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==
@@ Line 13: / Line 13: @@
 [[Category: Eucommia ulmoides]]
 [[Category: Single protein]]
-[[Category: Huang, R.H.]]
+[[Category: Huang, R H.]]
-[[Category: Tu, G.Z.]]
+[[Category: Tu, G Z.]]
-[[Category: Wang, D.C.]]
+[[Category: Wang, D C.]]
 [[Category: Xiang, Y.]]
 [[Category: Zhang, Y.]]
@@ Line 22: / Line 22: @@
 [[Category: disulfide stabilized motif]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:37:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:43 2008''