Quaternary structure of the small amino acid transporter OprG from Pseudomonas aeruginosa.

ABSTRACT: Pseudomonas aeruginosa is an opportunistic human pathogen that causes nosocomial infections. The P. aeruginosa outer membrane contains specific porins that enable substrate uptake, with the outer membrane protein OprG facilitating transport of small, uncharged amino acids. However, the pore size of an eight-stranded β-barrel monomer of OprG is too narrow to accommodate even the smallest transported amino acid, glycine, raising the question of how OprG facilitates amino acid uptake. Pro-92 of OprG is critically important for amino acid transport, with a P92A substitution inhibiting transport and the NMR structure of this variant revealing that this substitution produces structural changes in the barrel rim and restricts loop motions. OprG may assemble into oligomers in the out

SUBMITTER: Sanganna Gari RR 

PROVIDER: S-EPMC6222097 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature