8QXP

Crystal structure of the outer membrane porin OmpW from Klebsiella pneumoniae

Summary for 8QXP

• Entry DOI: 10.2210/pdb8qxp/pdb
• Descriptor: OmpW protein, SULFATE ION (2 entities in total)
• Functional Keywords: outer membrane porin, membrane protein
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 20970.33

Authors

Seddon, C.,Beis, K. (deposition date: 2023-10-24, release date: 2024-01-24)

Primary citation

Seddon, C.,Frankel, G.,Beis, K.
Structure of the outer membrane porin OmpW from the pervasive pathogen Klebsiella pneumoniae.
Acta Crystallogr.,Sect.F, 80:22-27, 2024

PubMed Abstract: Conjugation is the process by which plasmids, including those that carry antibiotic-resistance genes, are mobilized from one bacterium (the donor) to another (the recipient). The conjugation efficiency of IncF-like plasmids relies on the formation of mating-pair stabilization via intimate interactions between outer membrane proteins on the donor (a plasmid-encoded TraN isoform) and recipient bacteria. Conjugation of the R100-1 plasmid into Escherichia coli and Klebsiella pneumoniae (KP) recipients relies on pairing between the plasmid-encoded TraNα in the donor and OmpW in the recipient. Here, the crystal structure of K. pneumoniae OmpW (OmpW) is reported at 3.2 Å resolution. OmpW forms an eight-stranded β-barrel flanked by extracellular loops. The structures of E. coli OmpW (OmpW) and OmpW show high conservation despite sequence variability in the extracellular loops.

PubMed: 38206593
DOI: 10.1107/S2053230X23010579

Experimental method

X-RAY DIFFRACTION (3.2 Å)