Retraction Note: Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus
Autor: | Guan Zheng Luo, Jenny Winjing Quang, Quanjiang Ji, Hoonsik Cho, Taeok Bae, Kunqian Yu, Qiancheng You, Guangrong Qin, Xiaocheng Weng, Xin Deng, Peter J. Chen, Zdzislaw Wawrzak, Ziyang Hao, Won Sik Yeo, Chi Hao Luan, Xiaojing Yang, Hualiang Jiang, Chuan He |
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Rok vydání: | 2017 |
Předmět: |
030110 physiology
0301 basic medicine Staphylococcus aureus Transcription Genetic Science General Physics and Astronomy Crystallography X-Ray medicine.disease_cause General Biochemistry Genetics and Molecular Biology Small Molecule Libraries Benzophenones 03 medical and health sciences Bacterial Proteins Component (UML) medicine Multidisciplinary Chemistry Mechanism (biology) Gene Expression Regulation Bacterial General Chemistry Retraction Protein Structure Tertiary Mutation Biophysics Mutant Proteins Signal transduction Signal Transduction |
Zdroj: | Nature Communications Nature Communications, Vol 8, Iss 1, Pp 1-1 (2017) |
ISSN: | 2041-1723 |
DOI: | 10.1038/ncomms14331 |
Popis: | Most low GC Gram-positive bacteria possess an essential walKR two-component system (TCS) for signal transduction involved in regulating cell wall homoeostasis. Despite the well-established intracellular regulatory mechanism, the role of this TCS in extracellular signal recognition and factors that modulate the activity of this TCS remain largely unknown. Here we identify the extracellular receptor of the kinase 'WalK' (erWalK) as a key hub for bridging extracellular signal input and intracellular kinase activity modulation in Staphylococcus aureus. Characterization of the crystal structure of erWalK revealed a canonical Per-Arnt-Sim (PAS) domain for signal sensing. Single amino-acid mutation of potential signal-transduction residues resulted in severely impaired function of WalKR. A small molecule derived from structure-based virtual screening against erWalK is capable of selectively activating the walKR TCS. The molecular level characterization of erWalK will not only facilitate exploration of natural signal(s) but also provide a template for rational design of erWalK inhibitors. |
Databáze: | OpenAIRE |
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