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Carvalho, AL, A. Goyal, JAM Prates, DN Bolam, HJ Gilbert, VMR Pires, LMA Ferreira, A. Planas, MJ Romao, and CMGA Fontes. "The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site." Journal of Biological Chemistry. 279 (2004): 34785-34793. Abstract
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Santos-Silva, T., J. Trincao, AL Carvalho, C. Bonifacio, F. Auchere, P. Raleiras, I. Moura, JJG Moura, and MJ Romao. "The first crystal structure of class III superoxide reductase from Treponema pallidum." Journal of Biological Inorganic Chemistry. 11 (2006): 548-558. Abstract
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Pinheiro, B. A., J. L. A. Bras, S. Najmudin, AL Carvalho, LMA Ferreira, JAM Prates, and CMGA Fontes. "Flexibility and specificity of the cohesin-dockerin interaction: implications for cellulosome assembly and functionality." Biocatalysis and Biotransformation. 30 (2012): 309-315. AbstractWebsite

Cellulosomes are highly elaborate multi-enzyme complexes of Carbohydrate Active enZYmes (CAZYmes) secreted by cellulolytic microorganisms, which very effectively degrade the most abundant polymers on Earth, cellulose and hemicelluloses. Cellulosome assembly requires that a non-catalytic dockerin module found in cellulosomal enzymes binds to one of the various cohesin domains located in a large molecular scaffold called Scaffoldin. A diversity of cohesin -dockerin binding specificities have been described, the combination of which may result in complex plant cell wall degrading systems, maximising the synergy between enzymes in order to improve catalytic efficiency. Structural studies have allowed the spatial flexibility inherent to the cellulosomal system to be determined. Recent progress achieved from the study of the fundamental cohesin and dockerin units involved in cellulosome assembly will be reviewed.