Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
The major outer membrane protein OprG of Pseudomonas aeruginosa contributes to cytotoxicity and forms an anaerobically regulated, cation-selective channel.
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Purified OprG forms cation-selective channels in planar bilayers; it is ANR-induced anaerobically and is not involved in iron or antibiotic uptake.
"Planar bilayer studies indicated that purified OprG formed cationic-selective channels with a conductance of 500 pS in 1 M KCl"
The crystal structure of OprG from Pseudomonas aeruginosa, a potential channel for transport of hydrophobic molecules across the outer membrane.
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Crystal structure of OprG, an eight-stranded beta-barrel with a hydrophobic channel.
"OprG forms an eight-stranded β-barrel with a hydrophobic channel that leads from the extracellular surface to a lateral opening in the barrel wall."
OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.
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Reconstituted OprG transports small amino acids, confirmed by growth assays; NMR structures show flexible extracellular loops and no lateral gate.
"we reconstituted the purified protein into liposomes and found it to facilitate the transport of small amino acids such as glycine, alanine, valine, and serine, which was confirmed by Pseudomonas growth assays."