Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus

The WalKR signal transduction system is involved in extracellular signal recognition, but the details of this function are not well established. Here, the authors report the crystal structure of this two-component system alongside the characterisation of a small-molecule activator.

Bibliographic Details
Main Authors: Quanjiang Ji, Peter J. Chen, Guangrong Qin, Xin Deng, Ziyang Hao, Zdzislaw Wawrzak, Won-Sik Yeo, Jenny Winjing Quang, Hoonsik Cho, Guan-Zheng Luo, Xiaocheng Weng, Qiancheng You, Chi-Hao Luan, Xiaojing Yang, Taeok Bae, Kunqian Yu, Hualiang Jiang, Chuan He
Format: Article
Language:English
Published: Nature Publishing Group 2016-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms11000
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spelling doaj-982278f7c02745b09c2db25ee3867b432021-05-11T10:34:55ZengNature Publishing GroupNature Communications2041-17232016-03-017111110.1038/ncomms11000Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureusQuanjiang Ji0Peter J. Chen1Guangrong Qin2Xin Deng3Ziyang Hao4Zdzislaw Wawrzak5Won-Sik Yeo6Jenny Winjing Quang7Hoonsik Cho8Guan-Zheng Luo9Xiaocheng Weng10Qiancheng You11Chi-Hao Luan12Xiaojing Yang13Taeok Bae14Kunqian Yu15Hualiang Jiang16Chuan He17Department of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of SciencesDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoSynchrotron Research Center, LS-CAT, Northwestern UniversityIndiana University School of Medicine-NorthwestDepartment of Molecular Biosciences, High-Throughput Analysis Laboratory, Center for Structural Genomics of Infectious Diseases, Northwestern UniversityIndiana University School of Medicine-NorthwestDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoDepartment of Molecular Biosciences, High-Throughput Analysis Laboratory, Center for Structural Genomics of Infectious Diseases, Northwestern UniversityDepartment of Biochemistry and Molecular Biology, University of ChicagoIndiana University School of Medicine-NorthwestState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of SciencesState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of SciencesDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of ChicagoThe WalKR signal transduction system is involved in extracellular signal recognition, but the details of this function are not well established. Here, the authors report the crystal structure of this two-component system alongside the characterisation of a small-molecule activator.https://doi.org/10.1038/ncomms11000
collection DOAJ
language English
format Article
sources DOAJ
author Quanjiang Ji
Peter J. Chen
Guangrong Qin
Xin Deng
Ziyang Hao
Zdzislaw Wawrzak
Won-Sik Yeo
Jenny Winjing Quang
Hoonsik Cho
Guan-Zheng Luo
Xiaocheng Weng
Qiancheng You
Chi-Hao Luan
Xiaojing Yang
Taeok Bae
Kunqian Yu
Hualiang Jiang
Chuan He
spellingShingle Quanjiang Ji
Peter J. Chen
Guangrong Qin
Xin Deng
Ziyang Hao
Zdzislaw Wawrzak
Won-Sik Yeo
Jenny Winjing Quang
Hoonsik Cho
Guan-Zheng Luo
Xiaocheng Weng
Qiancheng You
Chi-Hao Luan
Xiaojing Yang
Taeok Bae
Kunqian Yu
Hualiang Jiang
Chuan He
Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
Nature Communications
author_facet Quanjiang Ji
Peter J. Chen
Guangrong Qin
Xin Deng
Ziyang Hao
Zdzislaw Wawrzak
Won-Sik Yeo
Jenny Winjing Quang
Hoonsik Cho
Guan-Zheng Luo
Xiaocheng Weng
Qiancheng You
Chi-Hao Luan
Xiaojing Yang
Taeok Bae
Kunqian Yu
Hualiang Jiang
Chuan He
author_sort Quanjiang Ji
title Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
title_short Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
title_full Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
title_fullStr Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
title_full_unstemmed Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
title_sort structure and mechanism of the essential two-component signal-transduction system walkr in staphylococcus aureus
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-03-01
description The WalKR signal transduction system is involved in extracellular signal recognition, but the details of this function are not well established. Here, the authors report the crystal structure of this two-component system alongside the characterisation of a small-molecule activator.
url https://doi.org/10.1038/ncomms11000
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