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TitleInteractions of outer membrane lipoproteins PA3214 and PqiC with their MCE protein binding partners, PA3213 and PqiB.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateMay 10, 2026
AuthorsSabrina I Giacometti / Nicolas Coudray / Rachel L Redler / Gira Bhabha / Damian C Ekiert
PubMed AbstractMembers of the Mammalian Cell Entry (MCE) superfamily interact with other proteins to form diverse architectures for the transport of hydrophobic molecules across the cell envelope in Gram-negative ...Members of the Mammalian Cell Entry (MCE) superfamily interact with other proteins to form diverse architectures for the transport of hydrophobic molecules across the cell envelope in Gram-negative bacteria. Some of these trans-envelope MCE protein complexes include a PqiC-like outer membrane (OM) lipoprotein component. The best-studied member of this group of OM lipoproteins is PqiC, from the PqiABC system, which can form an octameric ring. How PqiC-like lipoproteins interact with their MCE protein binding partners to facilitate transport is not well understood. Here we report the cryo-electron microscopy structures of PA3214, a homolog of PqiC, in the context of the full MCE transport PA3211-PA3214 system. Our structure provides insight into the biological assembly of the lipoprotein and interactions with its binding partner, MCE protein PA3213. We utilize deep mutational scanning to identify functionally important sites in PqiC in an unbiased manner. Through phenotypic and biochemical experiments, we characterize the interactions of the lipoproteins PqiC and PA3214 with their associated MCE proteins PqiB and PA3213, thus providing a model for how some MCE proteins employ a C-terminal peptide to mediate key interactions with their cognate lipoproteins at the OM.
External linksbioRxiv / PubMed:42146607 / PubMed Central
MethodsEM (single particle)
Resolution2.67 - 12.0 Å
Structure data

77071

13hq

EMDB-77071, PDB-13hq:
Cryo-EM structure of Pseudomonas aeruginosa soluble lipoprotein PA3214
Method: EM (single particle) / Resolution: 2.67 Å

77072

13hr

EMDB-77072: Cryo-EM structure of Pseudomonas aeruginosa outer-membrane lipoprotein PA3214 bound to MCE protein PA3213 C-terminal peptide (CASP target)
PDB-13hr: Cryo-EM structure of Pseudomonas aeruginosa outer-membrane lipoprotein PA3214 bound to MCE protein PA3213 C-terminal peptide
Method: EM (single particle) / Resolution: 2.7 Å

77073

13hs

EMDB-77073, PDB-13hs:
Cryo-EM structure of Pseudomonas aeruginosa outer-membrane lipoprotein PA3214 in the open conformation
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-77074: PA3213 MCE protein in complex with PA3214 OM lipoprotein
Method: EM (single particle) / Resolution: 12.0 Å

Source
  • Pseudomonas aeruginosa (bacteria)
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsLIPID TRANSPORT / lipoprotein / Pseudomonas aeruginosa / MCE system / outer membrane lipoprotein

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