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.
Acta Crystallogr F Struct Biol Commun
; 70(Pt 8): 1065-7, 2014 Aug.
Article
em En
| MEDLINE
| ID: mdl-25084383
ABSTRACT
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 via highly ordered protein-protein interactions between cohesin modules located in a molecular scaffold and dockerin modules found in cellulosomal enzymes. Acetivibrio cellulolyticus 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 A. cellulolyticus has been purified and crystallized, and data were processed to a resolution of 1.57â
Å in the orthorhombic space group P212121.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Proteínas Cromossômicas não Histona
/
Proteínas de Ciclo Celular
/
Glicosídeo Hidrolases
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Portugal