Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB

Wesley Tien Chiang, Yao-Kai Chang, Wei-Han Hui, Shu-Wei Chang, Chen-Yi Liao, Yi-Chuan Chang, Chun-Jung Chen, Wei-Chen Wang, Chien-Chen Lai, Chun-Hsiung Wang, Siou-Ying Luo, Ya-Ping Huang, Shan-Ho Chou, Tzyy-Leng Horng, Ming-Hon Hou, Stephen P. Muench, Ren-Shiang Chen, Ming-Daw Tsai () and Nien-Jen Hu ()
Additional contact information
Wesley Tien Chiang: National Chung Hsing University
Yao-Kai Chang: Academia Sinica
Wei-Han Hui: National Taiwan University
Shu-Wei Chang: National Taiwan University
Chen-Yi Liao: National Chung Hsing University
Yi-Chuan Chang: National Chung Hsing University
Chun-Jung Chen: National Synchrotron Radiation Research Center
Wei-Chen Wang: National Chung Hsing University
Chien-Chen Lai: National Chung Hsing University
Chun-Hsiung Wang: Academia Sinica
Siou-Ying Luo: Academia Sinica
Ya-Ping Huang: Academia Sinica
Shan-Ho Chou: National Chung Hsing University
Tzyy-Leng Horng: Feng Chia University
Ming-Hon Hou: National Chung Hsing University
Stephen P. Muench: University of Leeds
Ren-Shiang Chen: Tunghai University
Ming-Daw Tsai: Academia Sinica
Nien-Jen Hu: National Chung Hsing University

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract The K+ uptake system KtrAB is essential for bacterial survival in low K+ environments. The activity of KtrAB is regulated by nucleotides and Na+. Previous studies proposed a putative gating mechanism of KtrB regulated by KtrA upon binding to ATP or ADP. However, how Na+ activates KtrAB and the Na+ binding site remain unknown. Here we present the cryo-EM structures of ATP- and ADP-bound KtrAB from Bacillus subtilis (BsKtrAB) both solved at 2.8 Å. A cryo-EM density at the intra-dimer interface of ATP-KtrA was identified as Na+, as supported by X-ray crystallography and ICP-MS. Thermostability assays and functional studies demonstrated that Na+ binding stabilizes the ATP-bound BsKtrAB complex and enhances its K+ flux activity. Comparing ATP- and ADP-BsKtrAB structures suggests that BsKtrB Arg417 and Phe91 serve as a channel gate. The synergism of ATP and Na+ in activating BsKtrAB is likely applicable to Na+-activated K+ channels in central nervous system.

Date: 2024
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DOI: 10.1038/s41467-024-48057-y

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