Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9H80

Structure of the outer membrane exopolysaccharide transporter PelBC

Summary for 9H80
Entry DOI10.2210/pdb9h80/pdb
EMDB information51916
DescriptorPelB, PelC, PHOSPHATIDYLETHANOLAMINE (3 entities in total)
Functional Keywordsexopolysaccharide, complex, acyl-chain, transport protein
Biological sourcePseudomonas aeruginosa
More
Total number of polymer chains13
Total formula weight379410.09
Authors
Benedens, M.,Rosales, C.,Beckmann, R.,Kedrov, A. (deposition date: 2024-10-28, release date: 2025-06-11, Last modification date: 2025-06-18)
Primary citationBenedens, M.,Rosales-Hernandez, C.,Straathof, S.A.P.,Loschwitz, J.,Berninghausen, O.,Maglia, G.,Beckmann, R.,Kedrov, A.
Assembly and the gating mechanism of the Pel exopolysaccharide export complex PelBC of Pseudomonas aeruginosa.
Nat Commun, 16:5249-5249, 2025
Cited by
PubMed Abstract: The pathogen Pseudomonas aeruginosa enhances its virulence and antibiotic resistance upon formation of durable biofilms. The exopolysaccharides Pel, Psl and alginate essentially contribute to the biofilm matrix, but their secretion mechanisms are barely understood. Here, we reveal the architecture of the outer membrane complex PelBC for Pel export, where the essential periplasmic ring of twelve lipoproteins PelC is mounted on top of the nanodisc-embedded β-barrel PelB. The PelC assembly is stabilized by electrostatic contacts with the periplasmic rim of PelB and via the membrane-anchored acyl chains. The negatively charged interior of the PelB β-barrel forms a route for the cationic Pel exopolysaccharide. The β-barrel is sealed at the extracellular side, but molecular dynamic simulations suggest that the short loop Plug-S is sufficiently flexible to open a tunnel for the exopolysaccharide transport. This gating model is corroborated by single-channel conductivity measurements, where a deletion of Plug-S renders a constitutively open β-barrel. Our structural and functional analysis offers a comprehensive view on this pathogenicity-relevant complex and suggests the route taken by the exopolysaccharide at the final secretion step.
PubMed: 40473691
DOI: 10.1038/s41467-025-60605-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon