In this section
@article{Seddon:2024:10.1107/S2053230X23010579,
author = {Seddon, C and Frankel, G and Beis, K},
doi = {10.1107/S2053230X23010579},
journal = {Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online},
pages = {22--27},
title = {Structure of the outer membrane porin OmpW from the pervasive pathogen Klebsiella pneumoniae},
url = {http://dx.doi.org/10.1107/S2053230X23010579},
volume = {80},
year = {2024}
}
TY - JOUR
AB - 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 (OmpWKP) is reported at 3.2Å resolution. OmpWKP forms an eight-stranded β-barrel flanked by extracellular loops. The structures of E. coli OmpW (OmpWEC) and OmpWKP show high conservation despite sequence variability in the extracellular loops.
AU - Seddon,C
AU - Frankel,G
AU - Beis,K
DO - 10.1107/S2053230X23010579
EP - 27
PY - 2024///
SN - 1744-3091
SP - 22
TI - Structure of the outer membrane porin OmpW from the pervasive pathogen Klebsiella pneumoniae
T2 - Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online
UR - http://dx.doi.org/10.1107/S2053230X23010579
UR - https://www.ncbi.nlm.nih.gov/pubmed/38206593
UR - http://hdl.handle.net/10044/1/108904
VL - 80
ER -
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