Overexpression, purification, crystallization and preliminary X‐ray characterization of the fourth scaffoldin A cohesin from Acetivibrio cellulolyticus in complex with a dockerin from a family 5 glycoside hydrolase. Issue 8 (1st August 2014)

• Record Type: Journal Article
• Authors: Bule, Pedro; Correia, Ana; Cameron, Kate; Alves, Victor D.; Cardoso, Vânia; Fontes, Carlos M. G. A.; Najmudin, Shabir
• Is Part Of: Acta crystallographica. Volume 70:Issue 8(2014:Aug.)
• Page Start: 1065
• Page End: 1067
• Publication Date: 2014-08-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14013181
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Cellulosomes are cell‐bound multienzyme complexes secreted by anaerobic bacteria that play a crucial role in carbon turnover by degrading plant cell walls to simple sugars. Integration of cellulosomal components occurs <italic>via</italic> highly ordered protein–protein interactions between cohesin modules located in a molecular scaffold and dockerin modules found in cellulosomal enzymes. <italic>Acetivibrio cellulolyticus</italic> possesses a 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 dockerin from a family 5 glycoside hydrolase (GH5), which was engineered to inactivate one of the two putative cohesin‐binding interfaces, complexed with one of the ScaA cohesins from <italic>A. cellulolyticus</italic> has been purified and crystallized, and data were processed to a resolution of 1.57 Å in the orthorhombic space group <italic>P</italic>2₁2₁2₁.</p> </abstract>