9o40 | pdb_00009o40

cryo-EM structure of TolQR conformation1 in SMA nanodiscs

spinqualitylabelsall models 9o40, resolution 2.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9o40 is a 7 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.92Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TOLQ_ECOLI Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:11722743). The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726). The system also appears to be required for the activity of several outer membrane-localized enzymes with cell wall remodeling activity (PubMed:32152098). Is involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA (PubMed:1683466, PubMed:3294803). Publication Abstract from PubMed The Tol-Pal system is essential for maintaining outer membrane (OM) stability during cell division in Gram-negative bacteria. The inner membrane complex TolQRA harnesses proton motive force (PMF) to establish transient interactions within the periplasm, thereby coordinating cell envelope remodeling and facilitating OM invagination at division sites. However, the precise mechanism remains unclear. Here, we present cryo-electron microscopy structures of Escherichia coli TolQRA in multiple conformational states at 2.92-3.52 A resolution, revealing rotary dynamics within the complex. Computational simulations reveal a proton-conductive channel comprising the putative proton-accepting residue Asp23 and the conserved polar residues Thr145 and Thr178, with monitored inter-residue distances providing support for a proton-driven rotary mechanism. Site-directed mutagenesis combined with functional assays validates the AlphaFold-predicted structure of the periplasmic domains of TolR and TolA, and further pinpoints critical residues required for complex function. Together, these findings advance our understanding of TolQRA-mediated proton transduction and offer new avenues for antibiotic drug development. Deciphering the molecular mechanism of the bacterial division motor TolQRA.,Shen C, Xie T, Luo Y, Zhao F, Wang X, Zhang Z, Pang J, Zhang J, Dong X, Chang S, Ding BS, Ying B, Chi W, Su Z, Zhou R, Tang X, Dong H Cell Discov. 2025 Nov 4;11(1):87. doi: 10.1038/s41421-025-00841-w. PMID:41184225 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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