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Article

Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C.

Biochemistry - 8 Apr 2008

Guo Su, Zhang Xin, Seaton Barbara A, Roberts Mary F

Abstract excerpt

The Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), an interfacial enzyme associated with prokaryotic infectivity, is activated by binding to zwitterionic surfaces, particularly phosphatidycholine (PC). Two tryptophan residues (Trp47 in the two-turn helix B and Trp242 in a disordered loop) at the rim of the barrel structure are critical for this interaction. The helix B region...

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Identifiers

PMID: 18345643
DOI: 10.1021/bi702269u
PMCID: PMC2906773

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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