ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Purification, crystallization and preliminary X-ray characterization of the Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 3 citations in OpenAlex.
- Cell-surface Attachment of Bacterial Multienzyme Complexes Involves Highly Dynamic Protein-Protein Anchors.The Journal of biological chemistry · 2015Article
- Overexpression, crystallization and preliminary X-ray characterization of Ruminococcus flavefaciens scaffoldin C cohesin in complex with a dockerin from an uncharacterized CBM-containing protein.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Purification, crystallization and preliminary X-ray characterization of the third ScaB cohesin in complex with an ScaA X-dockerin from Acetivibrio cellulolyticus.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The cellulosome, a highly elaborate extracellular multi-enzyme complex of cellulases and hemicellulases, is responsible for the efficient degradation of plant cell-wall carbohydrates by anaerobic microorganisms. Cohesin and dockerin recognition pairs are integral to the architecture of the cellulosome. Thus, type I cohesin:dockerins are important for attaching the modular enzymatic components to primary scaffoldins to form the cellulosome. In contrast, type II dockerins located in primary scaffoldins bind to anchoring scaffoldins, thus contributing to the cell-surface attachment of the entire complex. Since anchoring scaffoldins usually contain more than one type II cohesin, they contribute to the assembly of polycellulosomes. Acetivibrio cellulolyticus possesses an extremely complex cellulosome arrangement which is organized by a primary enzyme-binding scaffoldin (ScaA), two anchoring scaffoldins (ScaC and ScaD) and an unusual adaptor scaffoldin (ScaB). A ScaB dockerin mutated to inactivate one of the two putative cohesin-binding interfaces complexed with the ScaC cohesin from A. cellulolyticus has been purified and crystallized and data were collected from tetragonal and monoclinic crystal forms to resolutions of 1.5 and 6.0 Å, respectively.
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