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Article

Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.

The Journal of biological chemistry - 4 Apr 2003

McClain Mark S, Iwamoto Hideki, Cao Ping, Vinion-Dubiel Arlene D, Li Yi, Szabo Gabor, Shao Zhifeng, Cover Timothy L

Abstract excerpt

Helicobacter pylori secretes a toxin, VacA, that can form anion-selective membrane channels. Within a unique amino-terminal hydrophobic region of VacA, there are three tandem GXXXG motifs (defined by glycines at positions 14, 18, 22, and 26), which are characteristic of transmembrane dimerization sequences. The goals of the current study were to investigate whether these GXXXG motifs are required for membrane...

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PMID: 12562777
DOI: 10.1074/jbc.M212595200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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