Flexibility and specificity of the cohesindockerin interaction: Implications for cellulosome assembly and functionality

Benedita Andrade Pinheiro, Joana Luís Armada Brás, Shabir Najmudin, Ana Luísa Carvalho, Luís M. A. Ferreira, José A. M. Prates, Carlos Mendes Godinho Andrade Fontes

Research output: Contribution to journalReview article

4 Citations (Scopus)

Abstract

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 cohesindockerin 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.

Original languageEnglish
Pages (from-to)309-315
Number of pages7
JournalBiocatalysis And Biotransformation
Volume30
Issue number3
DOIs
Publication statusPublished - 1 May 2012

Keywords

  • Cellulosome
  • Cohesin
  • Dockerin
  • Multienzyme complexes
  • Nanomachines
  • Protein:protein interaction

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