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Purification, crystallization and preliminary X‐ray characterization of the third ScaB cohesin in complex with an ScaA X‐dockerin from Acetivibrio cellulolyticus
Author(s) -
Cameron Kate,
Alves Victor D.,
Bule Pedro,
Ferreira Luís M. A.,
Fontes Carlos M. G. A.,
Najmudin Shabir
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1400750x
Subject(s) - cohesin , cellulosome , chemistry , clostridium thermocellum , microbiology and biotechnology , biochemistry , enzyme , biology , dna , cellulase , chromatin
Interactions between cohesin and dockerin modules are critical for the formation of the cellulosome, which is responsible for the efficient degradation of plant cell‐wall carbohydrates by anaerobes. Type I dockerin modules found in modular enzymatic components interact with type I cohesins in primary scaffoldins, enabling the assembly of the multi‐enzyme complex. In contrast, type II dockerins located in primary scaffoldins bind to type II cohesins in adaptor scaffoldins or anchoring scaffoldins located at the bacterial envelope, contributing to the cell‐surface attachment of the entire complex. 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). An ScaA X‐dockerin mutated to inactivate one of the two putative cohesin‐binding interfaces complexed with the third ScaB cohesin from A. cellulolyticus has been purified and crystallized and data were collected to a resolution of 2.41 Å.