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  2. 合肥物质科学研究院
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  4. 中科院强磁场科学中心
Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD

文献类型：期刊论文

作者Zhang, Wei1; Yu, Jigang1; Zhang, Xuecheng1; Peng, Hui1; Li, Xinxin1; Zhang, Jiahai2; Sun, Hongbin3; Tu, Xiaoming2
刊名PROTEIN AND PEPTIDE LETTERS
出版日期2018
卷号25期号:4页码:362-367
关键词Starch binding domain molten globule ligand induced folding carbohydrate binding module family 69 AmyP nuclear magnetic resonance
ISSN号0929-8665
DOI10.2174/0929866525666180122145846
通讯作者Zhang, Xuecheng(turenzh@ahu.edu.cn) ; Peng, Hui(pph0259@126.com)
英文摘要AmyP is an alpha-amylase which shows preferential degradation to soluble starch. In this substrate preference its Starch Binding Domain (SBD), which was recently assigned to a new Carbohydrate Binding Module (CBM) family 69, plays an important role. In the present study, the SBD of AmyP (AmyP-SBD) was recombinantly expressed, purified, and structurally characterized. Using Circular Dichroism (CD), intrinsic fluorescence, and nuclear magnetic resonance (NMR) spectroscopy, the structures of AmyP-SBD in the absence and presence of substrate analogue beta-cyclodextrin were measured. The results intriguingly showed that free form AmyP-SBD is partially unfolded, like a compact molten globule, and could be induced by the ligand to fold into a relatively rigid state. Further structure determination for folded AmyP-SBD revealed a topology distinctive from those of SBDs from other CBM families. Our data indicate AmyP-SBD is a structurally novel SBD, and this may be helpful for understanding the properties of AmyP-SBD and CBM69 and elucidation of functioning mechanism of AmyP.
WOS关键词ASPERGILLUS-NIGER GLUCOAMYLASE ; ALPHA-AMYLASE ENZYMES ; MOLTEN GLOBULE ; NMR ; HYDROLYSIS ; EVOLUTION ; PROTEINS ; GTPASE ; SYSTEM ; FAMILY
资助项目National Natural Science Foundation of China[31470775] ; Key Research Program of the Education Department of Anhui Province[KJ2014ZD01] ; International Science and Technology Cooperation Plan of Anhui Province[1503062010]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000435213800006
出版者BENTHAM SCIENCE PUBL LTD
资助机构National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Key Research Program of the Education Department of Anhui Province ; Key Research Program of the Education Department of Anhui Province ; Key Research Program of the Education Department of Anhui Province ; Key Research Program of the Education Department of Anhui Province ; 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源URL[http://ir.hfcas.ac.cn:8080/handle/334002/38185]  
专题合肥物质科学研究院_中科院强磁场科学中心
通讯作者Zhang, Xuecheng; Peng, Hui
作者单位1.Anhui Univ, Sch Life Sci, 111 Jiulong Rd, Hefei 230601, Anhui, Peoples R China
2.Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China
3.Chinese Acad Sci, Hefei Inst Phys Sci, High Magnet Field Lab, Hefei 230031, Anhui, Peoples R China
推荐引用方式
GB/T 7714		 Zhang, Wei,Yu, Jigang,Zhang, Xuecheng,et al. Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD[J]. PROTEIN AND PEPTIDE LETTERS,2018,25(4):362-367.
APA Zhang, Wei.,Yu, Jigang.,Zhang, Xuecheng.,Peng, Hui.,Li, Xinxin.,...&Tu, Xiaoming.(2018).Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD.PROTEIN AND PEPTIDE LETTERS,25(4),362-367.
MLA Zhang, Wei,et al."Ligand Induced Folding of the First Identified CBM69 Starch Binding Domain AmyP-SBD".PROTEIN AND PEPTIDE LETTERS 25.4(2018):362-367.

入库方式： OAI收割

来源：合肥物质科学研究院

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