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	Expulsion mechanism of the substrate-translocating subunit in ECF transporters.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 4484, Year 2023
Publish date	Jul 25, 2023
Authors	Chancievan Thangaratnarajah / Mark Nijland / Luís Borges-Araújo / Aike Jeucken / Jan Rheinberger / Siewert J Marrink / Paulo C T Souza / Cristina Paulino / Dirk J Slotboom /
PubMed Abstract	Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF ...Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogenic electron microscopy and reveal that ATP induces a concave-to-convex shape change of two long helices in the motor, thereby destroying the S-component's docking site and allowing for its dissociation. We show that adaptation of the membrane morphology to the conformational state of the motor may favour expulsion of the substrate-free S-component when ATP is bound and docking of the substrate-loaded S-component after hydrolysis. Our work provides a picture of bilayer-assisted chemo-mechanical coupling in the transport cycle of ECF transporters.
External links	Nat Commun / PubMed:37491368 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 4.3 Å
Structure data	16120 8bmp EMDB-16120, PDB-8bmp: Cryo-EM structure of the folate-specific ECF transporter complex in MSP2N2 lipid nanodiscs bound to ATP and ADP Method: EM (single particle) / Resolution: 3.2 Å 16121 8bmq EMDB-16121, PDB-8bmq: Cryo-EM structure of the folate-specific ECF transporter complex in MSP2N2 lipid nanodiscs bound to AMP-PNP Method: EM (single particle) / Resolution: 3.6 Å 16122 8bmr EMDB-16122, PDB-8bmr: Cryo-EM structure of the wild-type solitary ECF module in MSP2N2 lipid nanodiscs in the ATPase open and nucleotide-free conformation Method: EM (single particle) / Resolution: 3.8 Å EMDB-16123: Cryo-EM structure of the wild-type solitary ECF module in DDM micelles in the ATPase open and nucleotide-free conformation Method: EM (single particle) / Resolution: 4.3 Å 16124 8bms EMDB-16124, PDB-8bms: Cryo-EM structure of the mutant solitary ECF module 2EQ in MSP2N2 lipid nanodiscs in the ATPase closed and ATP-bound conformation Method: EM (single particle) / Resolution: 2.6 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-MG: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-HOH*: WATER / Water
Source	lactobacillus delbrueckii subsp. bulgaricus atcc 11842 = jcm 1002 (bacteria)
Keywords	MEMBRANE PROTEIN / ABC Transporter / ECF transporter complex / ATP / ADP / AMP-PNP / motor