globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1811518115
论文题名:
Snapshots of a modified nucleotide moving through the confines of a DNA polymerase
作者: Kropp H.M.; Dürr S.L.; Peter C.; Diederichs K.; Marx A.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:40
起始页码: 9992
结束页码: 9997
语种: 英语
英文关键词: Alkyne ; Click chemistryv ; Crystallography ; DNA polymerase ; Modified nucleotide
Scopus关键词: DNA polymerase ; nucleotide ; bacterial protein ; DNA ; DNA directed DNA polymerase beta ; Taq polymerase ; 3' untranslated region ; Article ; biochemical analysis ; chemical modification ; crystallization ; DNA synthesis ; enzyme activity ; enzyme conformation ; enzyme substrate ; molecular mechanics ; plasticity ; priority journal ; quantum mechanics ; structure analysis ; chemistry ; enzymology ; molecular model ; Thermus ; X ray crystallography ; Bacterial Proteins ; Crystallography, X-Ray ; DNA ; DNA Polymerase I ; Models, Molecular ; Taq Polymerase ; Thermus
英文摘要: DNA polymerases have evolved to process the four canonical nucleotides accurately. Nevertheless, these enzymes are also known to process modified nucleotides, which is the key to numerous core biotechnology applications. Processing of modified nucleotides includes incorporation of the modified nucleotide and postincorporation elongation to proceed with the synthesis of the nascent DNA strand. The structural basis for postincorporation elongation is currently unknown. We addressed this issue and successfully crystallized KlenTaq DNA polymerase in six closed ternary complexes containing the enzyme, the modified DNA substrate, and the incoming nucleotide. Each structure shows a high-resolution snapshot of the elongation of a modified primer, where the modification "moves" from the 3′-primer terminus upstream to the sixth nucleotide in the primer strand. Combining these data with quantum mechanics/molecular mechanics calculations and biochemical studies elucidates how the enzyme and the modified substrate mutually modulate their conformations without compromising the enzyme's activity significantly. The study highlights the plasticity of the system as origin of the broad substrate properties of DNA polymerases and facilitates the design of improved systems. © 2018 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163656
Appears in Collections:气候变化与战略

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作者单位: Kropp, H.M., Department of Chemistry, Universität Konstanz, Konstanz, 78464, Germany, Konstanz Research School Chemical Biology, Universität Konstanz, Konstanz, 78464, Germany; Dürr, S.L., Department of Chemistry, Universität Konstanz, Konstanz, 78464, Germany; Peter, C., Department of Chemistry, Universität Konstanz, Konstanz, 78464, Germany, Konstanz Research School Chemical Biology, Universität Konstanz, Konstanz, 78464, Germany; Diederichs, K., Konstanz Research School Chemical Biology, Universität Konstanz, Konstanz, 78464, Germany, Department of Biology, Universität Konstanz, Konstanz, 78464, Germany; Marx, A., Department of Chemistry, Universität Konstanz, Konstanz, 78464, Germany, Konstanz Research School Chemical Biology, Universität Konstanz, Konstanz, 78464, Germany

Recommended Citation:
Kropp H.M.,Dürr S.L.,Peter C.,et al. Snapshots of a modified nucleotide moving through the confines of a DNA polymerase[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(40)
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