A cellulosomal double-dockerin module from Clostridium thermocellum shows distinct structural and cohesin-binding features.

ABSTRACT: Cellulosomes are intricate cellulose-degrading multi-enzymatic complexes produced by anaerobic bacteria, which are valuable for bioenergy development and biotechnology. Cellulosome assembly relies on the selective interaction between cohesin modules in structural scaffolding proteins (scaffoldins) and dockerin modules in enzymes. Although the number of tandem cohesins in the scaffoldins is believed to determine the complexity of the cellulosomes, tandem dockerins also exist, albeit very rare, in some cellulosomal components whose assembly and functional roles are currently unclear. In this study, we characterized the structure and mode of assembly of a tandem bimodular double-dockerin, which is connected to a putative S8 protease in the cellulosome-producing bacterium, Clostridium thermoce

SUBMITTER: Chen C 

PROVIDER: S-EPMC10949318 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature