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  • Title: Escherichia coli expression, purification, crystallization, and structure determination of bacterial cohesin-dockerin complexes.
    Author: Brás JL, Carvalho AL, Viegas A, Najmudin S, Alves VD, Prates JA, Ferreira LM, Romão MJ, Gilbert HJ, Fontes CM.
    Journal: Methods Enzymol; 2012; 510():395-415. PubMed ID: 22608738.
    Abstract:
    Cellulosomes are highly efficient nanomachines that play a fundamental role during the anaerobic deconstruction of complex plant cell wall carbohydrates. The assembly of these complex nanomachines results from the very tight binding of repetitive cohesin modules, located in a noncatalytic molecular scaffold, and dockerin domains located at the C-terminus of the enzyme components of the cellulosome. The number of enzymes found in a cellulosome varies but may reach more than 100 catalytic subunits if cellulosomes are further organized in polycellulosomes, through a second type of cohesin-dockerin interaction. Structural studies have revealed how the cohesin-dockerin interaction mediates cellulosome assembly and cell-surface attachment, while retaining the flexibility required to potentiate catalytic synergy within the complex. Methods that might be applied for the production, purification, and structure determination of cohesin-dockerin complexes are described here.
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