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Article

Combined Crystal Structure of a Type I Cohesin: MUTATION AND AFFINITY BINDING STUDIES REVEAL STRUCTURAL DETERMINANTS OF COHESIN-DOCKERIN SPECIFICITIES.

The Journal of biological chemistry - 26 Jun 2015

Cameron Kate, Weinstein Jonathan Y, Zhivin Olga, Bule Pedro, Fleishman Sarel J, Alves Victor D, Gilbert Harry J, Ferreira Luís M A, Fontes Carlos M G A, Bayer Edward A, Najmudin Shabir

Abstract excerpt

Cohesin-dockerin interactions orchestrate the assembly of one of nature's most elaborate multienzyme complexes, the cellulosome. Cellulosomes are produced exclusively by anaerobic microbes and mediate highly efficient hydrolysis of plant structural polysaccharides, such as cellulose and hemicellulose. In the canonical model of cellulosome assembly, type I dockerin modules of the enzymes bind to reiterated type I...

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Identifiers

PMID: 25934389
DOI: 10.1074/jbc.M115.653303
PMCID: PMC4481221

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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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Combined Crystal Structure of a Type I Cohesin: MUTATION AND AFFINITY BINDING STUDIES REVEAL STRUCTURAL DETERMINANTS OF COHESIN-DOCKERIN SPECIFICITIES.PMID 25934389Read ↗

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