Article Metrics


Online attention

Purification, crystallization and preliminary X-ray characterization of the Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin

DOI: 10.1107/S1744309112031922 DOI Help
PMID: 22949188 PMID Help

Authors: Shabir Najmudin (Universidade Técnica de Lisboa) , Kate Cameron (Universidade Técnica de Lisboa, Portugal) , Victor Alves (CIISA – Faculdade de Medicina Veterinária) , Pedro Bule (Universidade Técnica de Lisboa, Portugal) , Luis. M. Ferreira (Universidade Técnica de Lisboa, Portugal) , Carlos M. G. A. Fontes (Universidade Técnica de Lisboa, Portugal) , Shabir Najmudin (Universidade Técnica de Lisboa, Portugal)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 68 , PAGES 1030-1033

State: Published (Approved)
Published: July 2012

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 compo- nents 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 puri\ufb01ed and crystallized and data were collected from tetragonal and monoclinic crystal \u02da forms to resolutions of 1.5 and 6.0 A, respectively.

Subject Areas: Biology and Bio-materials, Environment

Instruments: I04-Macromolecular Crystallography

Added On: 02/10/2012 17:49

Discipline Tags:

Technical Tags: