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TitleStructural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogen .
Journal, issue, pagesbioRxiv, Year 2024
Publish dateJun 19, 2024
AuthorsElina Karimullina / Yirui Guo / Hanif M Khan / Tabitha Emde / Bradley Quade / Rosa Di Leo / Zbyszek Otwinowski / D Tieleman Peter / Dominika Borek / Alexei Savchenko
PubMed AbstractGram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold the integrity of their cell envelope, an indispensable aspect for both division and survival. ...Gram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold the integrity of their cell envelope, 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-EM reconstructions of TolQ in apo and TolR- bound forms at atomic resolution. The apo TolQ configuration manifests as a symmetric pentameric pore, featuring a trans-membrane funnel leading towards a cytoplasmic chamber. In contrast, the TolQ-TolR complex assumes a proton non-permeable 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.
TEASER: Apo TolQ and TolQ-TolR structures depict structural rearrangements required for cell envelope organization in bacterial cell division.
External linksbioRxiv / PubMed:38948712 / PubMed Central
MethodsEM (single particle)
Resolution3.02 - 3.34 Å
Structure data

EMDB-43346, PDB-8vlw:
TolQ-TolR inner membrane protein complex from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.34 Å

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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