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学科主题物理化学
Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding
Yang, Ming-Jun1; Pang, Xue-Qin1; Zhang, Xin2; Han, Ke-Li1; Han KL(韩克利)
关键词Signal Recognition Particle Srp Gtpase Protein Targeting Reaction Chloroplast Srp System Protein-protein Interaction
刊名JOURNAL OF STRUCTURAL BIOLOGY
2011
ISSN待补充
DOI10.1016/j.jsb.2010.07.013
173期:1页:57-66
收录类别SCI
文章类型Article
部门归属11
项目归属1101
产权排名1,1
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]SIGNAL-RECOGNITION PARTICLE ; SRP-RECEPTOR INTERACTION ; CONFORMATIONAL-CHANGES ; ENDOPLASMIC-RETICULUM ; THYLAKOID MEMBRANES ; ATOMIC CHARGES ; MESH EWALD ; NG DOMAIN ; PROTEIN ; RNA
英文摘要Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding; Two GTPases in the signal recognition particle (SRP) and SRP receptor (SR) interact with one another to mediate the cotranslational protein targeting pathway. Previous studies have shown that a universally conserved SRP RNA facilitates an efficient SRP-SR interaction in the presence of a signal sequence bound to SRP. However, a remarkable exception has been found in chloroplast SRP (cpSRP) pathway, in which the SRP RNA is missing. Based on biochemical and structural analyses, it is proposed that free cpSRP receptor (cpFtsY) has already been preorganized into a closed state for efficient cpSRP-cpFtsY association. However, no direct evidence has been reported to support this postulation thus far. In this study, we characterized the structural dynamics of cpFtsY and its conformational rearrangements induced by GTP binding using molecular dynamics (MD) simulations. Our results showed that the GTP-binding event triggered substantial conformational changes in free cpFtsY, including the relative orientation of N-G domain and several conserved motifs that are critical in complex formation. These rearrangements enabled the cpFtsY to relax into a preorganized 'closed' state that favored the formation of a stable complex with cpSRP54. Interestingly, the intrinsic flexibility of alpha N1 helix facilitated these rearrangements. In addition, GTP binding in cpFtsY was mediated by conserved residues that have been shown in other SRP GTPases. These findings suggested that GTP-bound cpFtsY could fluctuate into conformations that are favorable to form the stable complex, providing explanation of why SRP-SR interaction bypasses the requirement of the SRP RNA at a molecular level. (C) 2010 Elsevier Inc. All rights reserved.
语种英语
WOS记录号WOS:000286123600007
引用统计
被引频次:19[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/115234
专题中国科学院大连化学物理研究所
通讯作者Han KL(韩克利)
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Dalian 116023, Liaoning, Peoples R China
2.CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
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Yang, Ming-Jun,Pang, Xue-Qin,Zhang, Xin,et al. Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding[J]. JOURNAL OF STRUCTURAL BIOLOGY,2011,173(1):57-66.
APA Yang, Ming-Jun,Pang, Xue-Qin,Zhang, Xin,Han, Ke-Li,&韩克利.(2011).Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding.JOURNAL OF STRUCTURAL BIOLOGY,173(1),57-66.
MLA Yang, Ming-Jun,et al."Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding".JOURNAL OF STRUCTURAL BIOLOGY 173.1(2011):57-66.
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