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DOI | 10.1126/science.aag2355 |
The role of dimer asymmetry and protomer dynamics in enzyme catalysis | |
Kim, Tae Hun1,8; Mehrabi, Pedram2,3; Ren, Zhong4,5; Sljoka, Adnan6; Ing, Christopher7,8; Bezginov, Alexandr2; Ye, Libin1; Pomes, Regis7,8; Prosser, R. Scott1,7; Pai, Emil F.2,3,7,9 | |
2017-01-20 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 355期号:6322 |
文章类型 | Article |
语种 | 英语 |
国家 | Canada; USA; Japan |
英文摘要 | Freeze-trapping x-ray crystallography, nuclear magnetic resonance, and computational techniques reveal the distribution of states and their interconversion rates along the reaction pathway of a bacterial homodimeric enzyme, fluoroacetate dehalogenase (FAcD). The crystal structure of apo-FAcD exhibits asymmetry around the dimer interface and cap domain, priming one protomer for substrate binding. This asymmetry is dynamically averaged through conformational exchange on a millisecond time scale. During catalysis, the protomer conformational exchange rate becomes enhanced, the empty protomer exhibits increased local disorder, and water egresses. Computational studies identify allosteric pathways between protomers. Water release and enhanced dynamics associated with catalysis compensate for entropic losses from substrate binding while facilitating sampling of the transition state. The studies provide insights into how substrate-coupled allosteric modulation of structure and dynamics facilitates catalysis in a homodimeric enzyme. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000392204800029 |
WOS关键词 | PARTICLE MESH EWALD ; DIHYDROFOLATE-REDUCTASE ; CONFORMATIONAL DYNAMICS ; ALLOSTERIC REGULATION ; PROTEIN-STRUCTURE ; NMR-SPECTROSCOPY ; STRUCTURAL BASIS ; COOPERATIVITY ; MECHANISM ; ENERGY |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/195267 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Toronto, Dept Chem, Mississauga, ON L5L 1C6, Canada; 2.Univ Toronto, Dept Med Biophys, Toronto, ON M5G 1L7, Canada; 3.Campbell Family Inst Canc Res, Princess Margaret Canc Ctr, Ontario Canc Inst, Toronto, ON M5G 1L7, Canada; 4.Univ Illinois, Dept Chem, Chicago, IL 60607 USA; 5.Renz Res Inc, Westmont, IL 60559 USA; 6.Kwansei Gakuin Univ, Sch Sci & Technol, Dept Informat, CREST,Japan Sci & Technol Agcy JST, Nishinomiya, Hyogo, Japan; 7.Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada; 8.Hosp Sick Children, Res Inst, Program Mol Struct & Funct, Toronto, ON M5G 1X8, Canada; 9.Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada |
推荐引用方式 GB/T 7714 | Kim, Tae Hun,Mehrabi, Pedram,Ren, Zhong,et al. The role of dimer asymmetry and protomer dynamics in enzyme catalysis[J]. SCIENCE,2017,355(6322). |
APA | Kim, Tae Hun.,Mehrabi, Pedram.,Ren, Zhong.,Sljoka, Adnan.,Ing, Christopher.,...&Pai, Emil F..(2017).The role of dimer asymmetry and protomer dynamics in enzyme catalysis.SCIENCE,355(6322). |
MLA | Kim, Tae Hun,et al."The role of dimer asymmetry and protomer dynamics in enzyme catalysis".SCIENCE 355.6322(2017). |
条目包含的文件 | 条目无相关文件。 |
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