Structural Studies on the Extracellular Domain of Sensor Histidine Kinase YycG from Staphylococcus aureus and Its Functional Implications
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- 作者：Truc Kim1 ; Jongkeun Choi2 ; Sangho Lee3 ; Kwon Joo Yeo4 ; Hae-Kap Cheong4 ; Kyeong Kyu Kim1 ; kyeongkyu@skku.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：TCS ; two-component system ; HK ; histidine kinase ; RR ; response regulator ; YycGex ; extracellular domain of YycG ; PAS ; Per-Arnt-Sim ; PDC ; PhoQ-DcuS-CitA ; MAD ; multiwavelength anomalous diffraction ; SeMet ; selenomethionine ; PASex ; extracellular PAS ; ET ; evolutionary trace ; Cu(Ph)3 ; 1 ; 10-phenanthroline-copper complex ; LB ; lysogeny broth ; SeMet-YycGex ; SeMet-substituted YycGex ; PBS ; phosphate-buffered saline ; BME ; β-mercaptoethanol
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3074-3089
- 全文大小：2781 K
文摘
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Extracellular domain of S. aureus YycG possesses a PAS/PDC fold.
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S. aureus YycG extracellular domain reveals two dimeric interfaces.
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S. aureus YycG HK is capable of forming multimers on the cell membrane.
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YycH and YycI cooperatively inhibit multimerization of YycG HK.
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This study improves our understanding of the properties of YycG HK.