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TitleStructural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogen .
Journal, issue, pagesSci Adv, Vol. 11, Issue 14, Page eadq9845, Year 2025
Publish dateApr 4, 2025
AuthorsElina Karimullina / Yirui Guo / Hanif M Khan / Tabitha Emde / Bradley Quade / Rosa Di Leo / Zbyszek Otwinowski / D Peter Tieleman / Dominika Borek / Alexei Savchenko /
PubMed AbstractGram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold cell envelope integrity, an indispensable aspect for both division and survival. The IM TolQ- ...Gram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold cell envelope integrity, an indispensable aspect for both division and survival. The IM TolQ-TolR complex is the essential part of the Tol-Pal system, serving as a conduit for PMF energy transfer to the outer membrane. Here we present cryo-electron microscopy reconstructions of TolQ in apo and TolR-bound forms at atomic resolution. The apo TolQ configuration manifests as a symmetric pentameric pore, featuring a transmembrane funnel leading toward a cytoplasmic chamber. In contrast, the TolQ-TolR complex assumes a proton nonpermeable stance, characterized by the TolQ pentamer's flexure to accommodate the TolR dimer, where two protomers undergo a translation-based relationship. Our structure-guided analysis and simulations support the rotor-stator mechanism of action, wherein the rotation of the TolQ pentamer harmonizes with the TolR protomers' interplay. These findings broaden our mechanistic comprehension of molecular stator units empowering critical functions within the Gram-negative bacterial cell envelope.
External linksSci Adv / PubMed:40184442 / PubMed Central
MethodsEM (single particle)
Resolution3.02 Å
Structure data

43902

9avi

EMDB-43902, PDB-9avi:
TolQ inner membrane protein from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.02 Å

Source
  • acinetobacter baumannii (bacteria)
KeywordsMEMBRANE PROTEIN / inner membrane protein complex / Structural Genomics / Center for Structural Biology of Infectious Diseases / CSBID

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