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

doi:10.1016/j.jsb.2004.04.002

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	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
通讯作者	dcwang@sun5.ibp.ac.cn
	2004-10-01
发表期刊	JOURNAL OF STRUCTURAL BIOLOGY
ISSN	1047-8477
卷号	148 期号:1 页码:86-97
摘要	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 Angstrom 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. (C) 2004 Elsevier Inc. All rights reserved.
关键词	Eucommia Antifungal Protein Atomic Resolution Crystallography Direct Methods Five-disulfide-bond Motif Structure-function Relationship
学科领域	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
DOI	10.1016/j.jsb.2004.04.002
收录类别	SCI
语种	英语
WOS记录号	WOS:000224065100007
引用统计
文献类型	期刊论文
条目标识符	http://ir.kib.ac.cn/handle/151853/13539
专题	离退休
作者单位	1.Chinese Acad Sci, Inst Biophys, Ctr Struct & Mol Biol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Kunming Inst Bot, Kunming 650204, Peoples R China
推荐引用方式 GB/T 7714	Xiang, Y,Huang, RH,Liu, XZ,et al. Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides - Oliver at an atomic resolution[J]. JOURNAL OF STRUCTURAL BIOLOGY,2004,148(1):86-97.
APA	Xiang, Y,Huang, RH,Liu, XZ,Zhang, Y,&Wang, DC.(2004).Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides - Oliver at an atomic resolution.JOURNAL OF STRUCTURAL BIOLOGY,148(1),86-97.
MLA	Xiang, Y,et al."Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides - Oliver at an atomic resolution".JOURNAL OF STRUCTURAL BIOLOGY 148.1(2004):86-97.

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