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	Inhibited KdpFABC transitions into an E1 off-cycle state.
Journal, issue, pages	Elife, Vol. 11, Year 2022
Publish date	Oct 18, 2022
Authors	Jakob M Silberberg / Charlott Stock / Lisa Hielkema / Robin A Corey / Jan Rheinberger / Dorith Wunnicke / Victor R A Dubach / Phillip J Stansfeld / Inga Hänelt / Cristina Paulino /
PubMed Abstract	KdpFABC is a high-affinity prokaryotic K uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K levels, KdpFABC needs to be ...KdpFABC is a high-affinity prokaryotic K uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K levels, KdpFABC needs to be inhibited to prevent excessive K accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES motif in the A domain of the pump subunit KdpB (KdpB). Here, we explore the structural basis of inhibition by KdpB phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC state that we termed E1P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1P state adopted by KdpFABC upon KdpB phosphorylation. The E1P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1P states to E2P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such states.
External links	Elife / PubMed:36255052 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 7.4 Å
Structure data	EMDB-14347: Cryo-EM map of the WT KdpFABC complex in the E2-P conformation, stabilised with the inhibitor orthovanadate Method: EM (single particle) / Resolution: 7.4 Å 14911 7zrd EMDB-14911, PDB-7zrd: Cryo-EM map of the WT KdpFABC complex in the E1-P tight conformation, stabilised with the inhibitor orthovanadate Method: EM (single particle) / Resolution: 3.3 Å 14912 7zre EMDB-14912, PDB-7zre: Cryo-EM map of the WT KdpFABC complex in the E1-P tight conformation, under turnover conditions Method: EM (single particle) / Resolution: 3.4 Å 14913 7zrg EMDB-14913, PDB-7zrg: Cryo-EM map of the WT KdpFABC complex in the E1_ATPearly conformation, under turnover conditions Method: EM (single particle) / Resolution: 3.5 Å 14914 7zrh EMDB-14914, PDB-7zrh: Cryo-EM structure of the KdpFABC complex in a nucleotide-free E1 conformation loaded with K+ Method: EM (single particle) / Resolution: 3.4 Å 14915 7zri EMDB-14915, PDB-7zri: Cryo-EM structure of the KdpFABC complex in a nucleotide-free E1 conformation loaded with K+ Method: EM (single particle) / Resolution: 3.5 Å 14916 7zrj EMDB-14916, PDB-7zrj: Cryo-EM structure of the KdpFABC complex in a nucleotide-free E1 conformation loaded with K+ Method: EM (single particle) / Resolution: 3.7 Å 14917 7zrk EMDB-14917, PDB-7zrk: Cryo-EM map of the WT KdpFABC complex in the E1-P_ADP conformation, under turnover conditions Method: EM (single particle) / Resolution: 3.1 Å 14918 7zrl EMDB-14918, PDB-7zrl: Cryo-EM map of the unphosphorylated KdpFABC complex in the E2-P conformation, under turnover conditions Method: EM (single particle) / Resolution: 4.0 Å 14919 7zrm EMDB-14919, PDB-7zrm: Cryo-EM map of the unphosphorylated KdpFABC complex in the E1-P_ADP conformation, under turnover conditions Method: EM (single particle) / Resolution: 3.7 Å
Chemicals	ChemComp-K: Unknown entry ChemComp-CDL: CARDIOLIPIN / phospholipidYM ChemComp-VO4: VANADATE ION ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG*: Unknown entry
Source	escherichia coli (E. coli) escherichia coli k-12 (bacteria)
Keywords	MEMBRANE PROTEIN / P-type ATPase / superfamily of K+ transporters (SKT) / potassium uptake system / off-cycle post-albers conformation / post-albers E1 conformation