8vp6 | pdb_00008vp6

Cryo-EM structure of the ABC transporter PCAT1 bound with Mg_class_2

spinqualitylabelsall models 8vp6, resolution 2.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vp6 is a 2 chain structure with sequence from Acetivibrio thermocellus ATCC 27405. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.97Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3DCU1_ACET2 Publication Abstract from PubMed 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. Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling.,Zhang R, Jagessar KL, Brownd M, Polasa A, Stein RA, Moradi M, Karakas E, Mchaourab HS Nat Commun. 2024 Oct 20;15(1):9055. doi: 10.1038/s41467-024-53420-0. PMID:39428489 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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