8Q2D

Crystal structure of the E. coli PqiC Lipoprotein residues 17-187

This is a non-PDB format compatible entry.

Summary for 8Q2D

• Entry DOI: 10.2210/pdb8q2d/pdb
• Related: 8Q2C
• Descriptor: Intermembrane transport lipoprotein PqiC (2 entities in total)
• Functional Keywords: outermembrane lipoprotein, transport protein
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 57361.01

Authors

Cooper, B.F.,Knowles, T.J. (deposition date: 2023-08-02, release date: 2023-09-20, Last modification date: 2024-01-31)

Primary citation

Cooper, B.F.,Ratkeviciute, G.,Clifton, L.A.,Johnston, H.,Holyfield, R.,Hardy, D.J.,Caulton, S.G.,Chatterton, W.,Sridhar, P.,Wotherspoon, P.,Hughes, G.W.,Hall, S.C.,Lovering, A.L.,Knowles, T.J.
An octameric PqiC toroid stabilises the outer-membrane interaction of the PqiABC transport system.
Embo Rep., 25:82-101, 2024

PubMed Abstract: The E. coli Paraquat Inducible (Pqi) Pathway is a putative Gram-negative phospholipid transport system. The pathway comprises three components: an integral inner membrane protein (PqiA), a periplasmic spanning MCE family protein (PqiB) and an outer membrane lipoprotein (PqiC). Interactions between all complex components, including stoichiometry, remain uncharacterised; nevertheless, once assembled into their quaternary complex, the trio of Pqi proteins are anticipated to provide a continuous channel between the inner and outer membranes of diderms. Here, we present X-ray structures of both the native and a truncated, soluble construct of the PqiC lipoprotein, providing insight into its biological assembly, and utilise neutron reflectometry to characterise the nature of the PqiB-PqiC-membrane interaction. Finally, we employ phenotypic complementation assays to probe specific PqiC residues, which imply the interaction between PqiB and PqiC is less intimate than previously anticipated.

PubMed: 38228789
DOI: 10.1038/s44319-023-00014-4

Experimental method

X-RAY DIFFRACTION (2.08 Å)