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Article

Structures of the Ultra-High-Affinity Protein-Protein Complexes of Pyocins S2 and AP41 and Their Cognate Immunity Proteins from Pseudomonas aeruginosa.

Journal of molecular biology - 28 Aug 2015

Joshi Amar, Grinter Rhys, Josts Inokentijs, Chen Sabrina, Wojdyla Justyna A, Lowe Edward D, Kaminska Renata, Sharp Connor, McCaughey Laura, Roszak Aleksander W, Cogdell Richard J, Byron Olwyn, Walker Daniel, Kleanthous Colin

Abstract excerpt

How ultra-high-affinity protein-protein interactions retain high specificity is still poorly understood. The interaction between colicin DNase domains and their inhibitory immunity (Im) proteins is an ultra-high-affinity interaction that is essential for the neutralisation of endogenous DNase catalytic activity and for protection against exogenous DNase bacteriocins. The colicin DNase-Im interaction is a model...

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Identifiers

PMID: 26215615
DOI: 10.1016/j.jmb.2015.07.014
PMCID: PMC4548480

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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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