1p9z: Difference between revisions
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'''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver''' | {{Structure | ||
|PDB= 1p9z |SIZE=350|CAPTION= <scene name='initialview01'>1p9z</scene> | |||
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'''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1P9Z is a [ | 1P9Z is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15147184 15147184] | ||
[[Category: Eucommia ulmoides]] | [[Category: Eucommia ulmoides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: disulfide stabilized motif]] | [[Category: disulfide stabilized motif]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:21:49 2008'' | ||
Revision as of 11:21, 20 March 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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