Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis and synergism of ATP and Na activation in bacterial K uptake system KtrAB.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 3850, Year 2024
Publish date	May 8, 2024
Authors	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 / Nien-Jen Hu /
PubMed 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 ...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.
External links	Nat Commun / PubMed:38719864 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.48 - 3.1 Å
Structure data	36800 8k1s EMDB-36800, PDB-8k1s: Potassium transporter KtrAB from Bacillus subtilis in ADP-bound state Method: EM (single particle) / Resolution: 2.83 Å EMDB-36801: Potassium transporter KtrAB from Bacillus subtilis in ADP-bound state, focused refined on KtrA octamer Method: EM (single particle) / Resolution: 2.84 Å EMDB-36802: Potassium transporter KtrAB from Bacillus subtilis in ADP-bound state, focused refined on KtrB dimer Method: EM (single particle) / Resolution: 2.86 Å 36803 8k1t EMDB-36803, PDB-8k1t: Potassium transporter KtrAB from Bacillus subtilis in ATP-bound state with addition of MgCl2 Method: EM (single particle) / Resolution: 2.48 Å 36804 8k1u EMDB-36804, PDB-8k1u: Potassium transporter KtrAB from Bacillus subtilis in ATP-bound state with addition of EDTA and EGTA Method: EM (single particle) / Resolution: 2.82 Å 38477 8xmh EMDB-38477, PDB-8xmh: Potassium transporter KtrAB from Bacillus subtilis in ATP-bound state with addition of EDTA and EGTA, vertical C2 symmetry axis Method: EM (single particle) / Resolution: 2.85 Å 38478 8xmi EMDB-38478, PDB-8xmi: Potassium transporter KtrAB from Bacillus subtilis in ATP-bound state with addition of EDTA and EGTA, C1 symmetry Method: EM (single particle) / Resolution: 3.0 Å PDB-8k16: KtrA bound with ATP and thallium Method: X-RAY DIFFRACTION / Resolution: 3.1 Å PDB-8k1k: KtrA bound with ATP and sodium Method: X-RAY DIFFRACTION / Resolution: 3.0 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-TL: THALLIUM (I) ION / Thallium ChemComp-NA: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-K: Unknown entry
Source	bacillus subtilis (bacteria)
Keywords	METAL TRANSPORT / potassium channel RCK domain / METAL BINDING PROTEIN / Potassium channel / TRANSPORT PROTEIN / KtrAB / RCK / potassium / transporter