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Article

Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F.

The Journal of biological chemistry - 3 Apr 2009

Schwarzer David, Stummeyer Katharina, Haselhorst Thomas, Freiberger Friedrich, Rode Bastian, Grove Melanie, Scheper Thomas, von Itzstein Mark, Mühlenhoff Martina, Gerardy-Schahn Rita

Abstract excerpt

Endosialidases (endoNs), as identified so far, are tailspike proteins of bacteriophages that specifically bind and degrade the alpha2,8-linked polysialic acid (polySia) capsules of their hosts. The crystal structure solved for the catalytic domain of endoN from coliphage K1F (endoNF) revealed a functional trimer. Folding of the catalytic trimer is mediated by an intramolecular C-terminal chaperone domain. Release...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19189967
DOI: 10.1074/jbc.M808475200
PMCID: PMC2666599

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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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