Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues

The DNA ligase of African swine fever virus is one of the most error-prone ligases identified to date, but underlying molecular details are lacking. Here, Chen et al. report four AsfvLIG:DNA structures and identify a unique N-terminal domain and four unique active site residues that are crucial for...

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Main Authors:	Yiqing Chen, Hehua Liu, Chun Yang, Yanqing Gao, Xiang Yu, Xi Chen, Ruixue Cui, Lina Zheng, Suhua Li, Xuhang Li, Jinbiao Ma, Zhen Huang, Jixi Li, Jianhua Gan
Format:	Article
Language:	English
Published:	Nature Publishing Group 2019-01-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-019-08296-w

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spelling	doaj-2bedf69d630b4905bf64d70caac45ee12021-05-11T12:28:58ZengNature Publishing GroupNature Communications2041-17232019-01-0110111310.1038/s41467-019-08296-wStructure of the error-prone DNA ligase of African swine fever virus identifies critical active site residuesYiqing Chen0Hehua Liu1Chun Yang2Yanqing Gao3Xiang Yu4Xi Chen5Ruixue Cui6Lina Zheng7Suhua Li8Xuhang Li9Jinbiao Ma10Zhen Huang11Jixi Li12Jianhua Gan13State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry, School of Life Sciences, Fudan UniversityCollege of Life Sciences, Sichuan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityState Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan UniversityThe DNA ligase of African swine fever virus is one of the most error-prone ligases identified to date, but underlying molecular details are lacking. Here, Chen et al. report four AsfvLIG:DNA structures and identify a unique N-terminal domain and four unique active site residues that are crucial for its catalytic efficiency.https://doi.org/10.1038/s41467-019-08296-w
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Yiqing Chen Hehua Liu Chun Yang Yanqing Gao Xiang Yu Xi Chen Ruixue Cui Lina Zheng Suhua Li Xuhang Li Jinbiao Ma Zhen Huang Jixi Li Jianhua Gan
spellingShingle	Yiqing Chen Hehua Liu Chun Yang Yanqing Gao Xiang Yu Xi Chen Ruixue Cui Lina Zheng Suhua Li Xuhang Li Jinbiao Ma Zhen Huang Jixi Li Jianhua Gan Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues Nature Communications
author_facet	Yiqing Chen Hehua Liu Chun Yang Yanqing Gao Xiang Yu Xi Chen Ruixue Cui Lina Zheng Suhua Li Xuhang Li Jinbiao Ma Zhen Huang Jixi Li Jianhua Gan
author_sort	Yiqing Chen
title	Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues
title_short	Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues
title_full	Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues
title_fullStr	Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues
title_full_unstemmed	Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues
title_sort	structure of the error-prone dna ligase of african swine fever virus identifies critical active site residues
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2019-01-01
description	The DNA ligase of African swine fever virus is one of the most error-prone ligases identified to date, but underlying molecular details are lacking. Here, Chen et al. report four AsfvLIG:DNA structures and identify a unique N-terminal domain and four unique active site residues that are crucial for its catalytic efficiency.
url	https://doi.org/10.1038/s41467-019-08296-w
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Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues

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