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	Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 9055, Year 2024
Publish date	Oct 20, 2024
Authors	Ruojing Zhang / Kevin L Jagessar / Matthew Brownd / Adithya Polasa / Richard A Stein / Mahmoud Moradi / Erkan Karakas / Hassane S Mchaourab /
PubMed Abstract	Protease-containing ABC transporters (PCATs) couple the energy of ATP hydrolysis to the processing and export of diverse cargo proteins across cell membranes to mediate antimicrobial resistance and ...Protease-containing ABC transporters (PCATs) couple the energy of ATP hydrolysis to the processing and export of diverse cargo proteins across cell membranes to mediate antimicrobial resistance and quorum sensing. Here, we combine biochemical analysis, single particle cryoEM, and DEER spectroscopy in lipid bilayers along with computational analysis to illuminate the structural and energetic underpinnings of coupled cargo protein export. Our integrated investigation uncovers competitive interplay between nucleotides and cargo protein binding that ensures the latter's orderly processing and subsequent transport. The energetics of cryoEM structures in lipid bilayers are congruent with the inferred mechanism from ATP turnover analysis and reveal a snapshot of a high-energy outward-facing conformation that provides an exit pathway into the lipid bilayer and/or the extracellular side. DEER investigation of the core ABC transporter suggests evolutionary tuning of the energetic landscape to fulfill the function of substrate processing prior to export.
External links	Nat Commun / PubMed:39428489 / PubMed Central
Methods	EM (single particle)
Resolution	2.96 - 3.48 Å
Structure data	43393 8vow EMDB-43393, PDB-8vow: Cryo-EM structure of the ABC transporter PCAT1 cysteine-free core bound with MgATP and Vi Method: EM (single particle) / Resolution: 3.44 Å 43394 8vox EMDB-43394, PDB-8vox: Cryo-EM structure of the ABC transporter PCAT1 cysteine-free core bound with MgADP Method: EM (single particle) / Resolution: 3.07 Å 43396 8voz EMDB-43396, PDB-8voz: Cryo-EM structure of the ABC transporter PCAT1 cysteine-free core bound with MgADP and substrate Method: EM (single particle) / Resolution: 3.03 Å 43398 8vp1 EMDB-43398, PDB-8vp1: Cryo-EM structure of the ABC transporter PCAT1 cysteine-free core bound with ATP Method: EM (single particle) / Resolution: 3.48 Å 43400 8vp3 EMDB-43400, PDB-8vp3: Cryo-EM structure of the ABC transporter PCAT1 bound with MgADP and Substrate Method: EM (single particle) / Resolution: 2.96 Å 43401 8vp5 EMDB-43401, PDB-8vp5: Cryo-EM structure of the ABC transporter PCAT1 bound with ADP and Substrate Method: EM (single particle) / Resolution: 3.18 Å 43402 8vp6 EMDB-43402, PDB-8vp6: Cryo-EM structure of the ABC transporter PCAT1 bound with Mg_class_2 Method: EM (single particle) / Resolution: 2.97 Å 43403 8vp8 EMDB-43403, PDB-8vp8: Cryo-EM structure of the ABC transporter PCAT1 bound with ATP and Substrate Method: EM (single particle) / Resolution: 3.37 Å 43404 8vp9 EMDB-43404, PDB-8vp9: Cryo-EM structure of the cysteine-free ABC transporter PCAT1 bound with ADP and Substrate Method: EM (single particle) / Resolution: 3.18 Å 43405 8vpa EMDB-43405, PDB-8vpa: Cryo-EM structure of the ABC transporter PCAT1 bound with ADP Method: EM (single particle) / Resolution: 3.11 Å 43406 8vpb EMDB-43406, PDB-8vpb: Cryo-EM structure of the ABC transporter PCAT1 bound with MgADP_Class_2 Method: EM (single particle) / Resolution: 3.23 Å 44015 9azl EMDB-44015, PDB-9azl: Cryo-EM structure of the ABC transporter PCAT1 bound with MgADP class1 Method: EM (single particle) / Resolution: 2.99 Å 44402 9baa EMDB-44402, PDB-9baa: Cryo-EM structure of the ABC transporter PCAT1 bound with Mg_class_1 Method: EM (single particle) / Resolution: 3.39 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-VO4: VANADATE ION PDB-1acx: ACTINOXANTHIN STRUCTURE AT THE ATOMIC LEVEL (RUSSIAN) ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM
Source	acetivibrio thermocellus atcc 27405 (bacteria)
Keywords	TRANSPORT PROTEIN / ABC transporter / Nucleotide / Membrane Protein