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Article

NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.

Journal of the American Chemical Society - 9 Oct 2013

Zhuang Tiandi, Chisholm Christina, Chen Min, Tamm Lukas K

Abstract excerpt

The outer membrane protein G (OmpG) is a monomeric 33 kDa 14-stranded β-barrel membrane protein functioning as a nonspecific porin for the uptake of oligosaccharides in Escherichia coli. Two different crystal structures of OmpG obtained at different values of pH suggest a pH-gated pore opening mechanism. In these structures, extracellular loop 6 extends away from the barrel wall at neutral pH but is folded back...

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Identifiers

PMID: 24020969
DOI: 10.1021/ja408206e
PMCID: PMC3863726

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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