Revisiting the NMR solution structure of the Ce148S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation

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	Revisiting the NMR solution structure of the Ce148S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation
	Chen, Chao 1,3; Cui, Zhenling 1,3; Xiao, Yan 1; Cui, Qiu 1,2; Smith, Steven P.4; Lamed, Raphael 5; Bayer, Edward A.6; Feng, Yingang 1
刊名	JOURNAL OF STRUCTURAL BIOLOGY
	2014-11-01
卷号	188 期号:2 页码:188-193
关键词	Protein structure Protein-protein interaction Cellulosome Dockerin Cohesin Cis-proline
英文摘要	Dockerin modules of the cellulosomal enzyme subunits play an important role in the assembly of the cellulosome by binding tenaciously to cohesin modules of the scaffoldin subunit. A previously reported NMR-derived solution structure of the type-I dockerin module from Ce148S of Clostridium thermocellum, which utilized two-dimensional homonuclear H-1-H-1 NOESY and three-dimensional N-15-edited NOESY distance restraints, displayed substantial conformational differences from subsequent structures of dockerin modules in complex with their cognate cohesin modules, raising the question whether the source of the observed differences resulted from cohesin-induced structural rearrangements. Here, we determined the solution structure of the Ce148S type-I dockerin based on N-15- and C-13-edited NOESY-derived distance restraints. The structure adopted a fold similar to X-ray crystal structures of dockerin modules in complex with their cohesin partners. A unique cis-peptide bond between Leu-65 and Pro-66 in the Ce148S type-I dockerin module was also identified in the present structure. Our structural analysis of the Ce148S type-I dockerin module indicates that it does not undergo appreciable cohesin-induced structural alterations but rather assumes an inherent calcium-dependent cohesin-primed conformation. (C) 2014 Elsevier Inc. All rights reserved.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
研究领域[WOS]	Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]	DUAL BINDING MODE ; PROTEIN STRUCTURES ; CRYSTAL-STRUCTURE ; NOE ASSIGNMENT ; CELLULOSOME ; DOMAIN ; SPECTROSCOPY ; DEGRADATION ; PREDICTION ; PROGRAM
收录类别	SCI
语种	英语
WOS记录号	WOS:000344839100012
公开日期	2015-12-24
内容类型	期刊论文
源URL	[http://ir.qibebt.ac.cn/handle/337004/6169]
专题	青岛生物能源与过程研究所_代谢物组学团队
作者单位	1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Qingdao 266101, Peoples R China 2.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Key Lab Biofuels, Qingdao 266101, Shandong, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Queens Univ, Dept Biomed & Mol Sci, Kingston, ON K7L 3N6, Canada 5.Tel Aviv Univ, Dept Mol Microbiol & Biotechnol, IL-69978 Tel Aviv, Israel 6.Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
推荐引用方式 GB/T 7714	Chen, Chao,Cui, Zhenling,Xiao, Yan,et al. Revisiting the NMR solution structure of the Ce148S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation[J]. JOURNAL OF STRUCTURAL BIOLOGY,2014,188(2):188-193.
APA	Chen, Chao.,Cui, Zhenling.,Xiao, Yan.,Cui, Qiu.,Smith, Steven P..,...&Feng, Yingang.(2014).Revisiting the NMR solution structure of the Ce148S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation.JOURNAL OF STRUCTURAL BIOLOGY,188(2),188-193.
MLA	Chen, Chao,et al."Revisiting the NMR solution structure of the Ce148S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation".JOURNAL OF STRUCTURAL BIOLOGY 188.2(2014):188-193.