1p9z: Difference between revisions

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[[Image:1p9z.gif|left|200px]]
{{Seed}}
[[Image:1p9z.png|left|200px]]


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{{STRUCTURE_1p9z|  PDB=1p9z  |  SCENE=  }}  
{{STRUCTURE_1p9z|  PDB=1p9z  |  SCENE=  }}  


'''The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver'''
===The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15147184}}


==About this Structure==
==About this Structure==
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].  
1P9Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eucommia_ulmoides Eucommia ulmoides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Z OCA].  


==Reference==
==Reference==
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[[Category: Chitin-binding peptide]]
[[Category: Chitin-binding peptide]]
[[Category: Disulfide stabilized motif]]
[[Category: Disulfide stabilized motif]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:52:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:49:40 2008''

Revision as of 13:49, 28 July 2008

File:1p9z.png

Template:STRUCTURE 1p9z

The Solution Structure of Antifungal Peptide Distinct With a Five-disulfide Motif from Eucommia ulmoides Oliver

Template:ABSTRACT PUBMED 15147184

About this Structure

1P9Z is a Single protein structure of sequence from Eucommia ulmoides. Full experimental 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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