9o40

From Proteopedia

(Difference between revisions)

Current revision

cryo-EM structure of TolQR conformation1 in SMA nanodiscs

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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cascales E, Lloubès R, Sturgis JN. The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Mol Microbiol. 2001 Nov;42(3):795-807. PMID:11722743 doi:10.1046/j.1365-2958.2001.02673.x
↑ Webster RE. The tol gene products and the import of macromolecules into Escherichia coli. Mol Microbiol. 1991 May;5(5):1005-11. PMID:1683466 doi:10.1111/j.1365-2958.1991.tb01873.x
↑ Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol Microbiol. 2007 Feb;63(4):1008-25. PMID:17233825 doi:10.1111/j.1365-2958.2006.05571.x
↑ Santos TM, Lin TY, Rajendran M, Anderson SM, Weibel DB. Polar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complex. Mol Microbiol. 2014 Jun;92(5):985-1004. PMID:24720726 doi:10.1111/mmi.12609
↑ Yakhnina AA, Bernhardt TG. The Tol-Pal system is required for peptidoglycan-cleaving enzymes to complete bacterial cell division. Proc Natl Acad Sci U S A. 2020 Mar 24;117(12):6777-6783. PMID:32152098 doi:10.1073/pnas.1919267117
↑ Sun TP, Webster RE. Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli. J Bacteriol. 1987 Jun;169(6):2667-74. PMID:3294803 doi:10.1128/jb.169.6.2667-2674.1987
↑ Webster RE. The tol gene products and the import of macromolecules into Escherichia coli. Mol Microbiol. 1991 May;5(5):1005-11. PMID:1683466 doi:10.1111/j.1365-2958.1991.tb01873.x
↑ 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. Deciphering the molecular mechanism of the bacterial division motor TolQRA. Cell Discov. 2025 Nov 4;11(1):87. PMID:41184225 doi:10.1038/s41421-025-00841-w

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/9o40"

Categories: Escherichia coli str. K-12 substr. MG1655 | Large Structures | Luo YB | Shen CR

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9o40 is ON HOLD  until Paper Publication
+==cryo-EM structure of TolQR conformation1 in SMA nanodiscs==
+<StructureSection load='9o40' size='340' side='right'caption='[[9o40]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9o40]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9O40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9O40 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.92&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9o40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9o40 OCA], [https://pdbe.org/9o40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9o40 RCSB], [https://www.ebi.ac.uk/pdbsum/9o40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9o40 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TOLQ_ECOLI 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).<ref>PMID:11722743</ref> <ref>PMID:1683466</ref> <ref>PMID:17233825</ref> <ref>PMID:24720726</ref> <ref>PMID:32152098</ref> <ref>PMID:3294803</ref> <ref>PMID:1683466</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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<ref>PMID:41184225</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 9o40" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli str. K-12 substr. MG1655]]
+[[Category: Large Structures]]
+[[Category: Luo YB]]
+[[Category: Shen CR]]

9o40

From Proteopedia

Current revision

cryo-EM structure of TolQR conformation1 in SMA nanodiscs

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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