8bms | pdb_00008bms

Cryo-EM structure of the mutant solitary ECF module 2EQ in MSP2N2 lipid nanodiscs in the ATPase closed and ATP-bound conformation

spinqualitylabelsall models 8bms, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bms is a 3 chain structure with sequence from Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 = JCM 1002. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.6Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ECFA1_LACDA ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. Publication Abstract from PubMed 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. Expulsion mechanism of the substrate-translocating subunit in ECF transporters.,Thangaratnarajah C, Nijland M, Borges-Araujo L, Jeucken A, Rheinberger J, Marrink SJ, Souza PCT, Paulino C, Slotboom DJ Nat Commun. 2023 Jul 25;14(1):4484. doi: 10.1038/s41467-023-40266-1. PMID:37491368 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA