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Article

The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization.

Protein science : a publication of the Protein Society - 1 Apr 2002

Kreisberg Jason F, Betts Scott D, Haase-Pettingell Cameron, King Jonathan

Abstract excerpt

The P22 tailspike adhesin is an elongated thermostable trimer resistant to protease digestion and to denaturation in sodium dodecyl sulfate. Monomeric, dimeric, and protrimeric folding and assembly intermediates lack this stability and are thermolabile. In the native trimer, three right-handed parallel beta-helices (residues 143-540), pack side-by-side around the three-fold axis. After residue 540, these single...

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Identifiers

PMID: 11910025
DOI: 10.1110/ps.3440102
PMCID: PMC2373520

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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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