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Lookup NU author(s): Benedita Pinheiro, Kate Cameron, Dr Fiona Cuskin, Emeritus Professor Harry Gilbert
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
During the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.
Author(s): Bras JLA, Pinheiro BA, Cameron K, Cuskin F, Viegas A, Najmudin S, Bule P, Pires VMR, Romao MJ, Bayer EA, Spencer HL, Smith S, Gilbert HJ, Alves VD, Carvalho AL, Fontes CMGA
Publication type: Article
Publication status: Published
Journal: Scientific Reports
Year: 2016
Volume: 6
Online publication date: 07/12/2016
Acceptance date: 07/11/2016
Date deposited: 02/02/2017
ISSN (print): 2045-2322
Publisher: Nature Publishing Group
URL: http://dx.doi.org/10.1038/srep38292
DOI: 10.1038/srep38292
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