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1p9g

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{{STRUCTURE_1p9g| PDB=1p9g | SCENE= }}
{{STRUCTURE_1p9g| PDB=1p9g | SCENE= }}
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'''Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Ecommia ulmoides Oliver at atomic resolution'''
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===Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Ecommia ulmoides Oliver at atomic resolution===
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==Overview==
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EAFP2 is a novel antifungal protein isolated from the bark of the tree Eucommia ulmoides Oliver. It consists of 41 residues and is characterized with a five-disulfide motif and the inhibitory effects on the growth of both cell wall chitin-containing and chitin-free fungi. The crystal structure of EAFP2 at an atomic resolution of 0.84 A has been determined by using Shake-and-Bake direct methods with the program SnB. The phases obtained were of sufficient quality to permit the initial model built automatically and the structural refinement carried out using anisotropic displacement parameters resulted in a final crystallographic R factor of 6.8%. In the resulting structural model, all non-hydrogen protein atoms including an unusual pyroglutamyl acid residue at the N-terminal can fit to the articulated electron densities with one centre and more than 65% of the hydrogen atoms in the protein can be observed as individual peaks in the difference map. The general fold of EAFP2 is composed of a 3(10) helix (Cys3-Arg6), an alpha-helix (Ala27-Cys31) and a three-stranded antiparallel beta-sheet (Cys16-Ser18, Cys23-Ser25, and Cys35-Cys37) and cross-linked by five disulfide bridges. The tertiary structure of EAFP2 can be divided into two structural sectors, A and B. Sector A composed of residues 11-30 adopts a conformation similar to the chitin-binding domain in the hevein-like proteins and features a hydrophobic surface embraced a chitin-binding site (Tyr20, 22, 29, and Ser18). The distinct disulfide bridge Cys7-Cys37 connects the N-terminal ten residues with the C-terminal segment 35-41 to form the sector B, which features a cationic surface distributing all four positively charged residues, Arg6, 9, 36, and 40. Based on these structural features, the possible structural basis of the functional properties of EAFP2 is discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 15363789 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15363789}}
==About this Structure==
==About this Structure==
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[[Category: Antifungal peptide]]
[[Category: Antifungal peptide]]
[[Category: Atomic resolution]]
[[Category: Atomic resolution]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:50:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:15:33 2008''

Revision as of 08:15, 28 July 2008

Image:1p9g.png

Template:STRUCTURE 1p9g

Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Ecommia ulmoides Oliver at atomic resolution

Template:ABSTRACT PUBMED 15363789

About this Structure

1P9G is a Single protein structure of sequence from Eucommia ulmoides. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution., Xiang Y, Huang RH, Liu XZ, Zhang Y, Wang DC, J Struct Biol. 2004 Oct;148(1):86-97. PMID:15363789

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