Open AccessPurification and crystallization of a multimodular heterotrimeric complex containing both type I and type II cohesin–dockerin interactions from the cellulosome of Clostridium thermocellum
Author(s) -
Currie Mark A.,
Adams Jarrett J.,
Ali Sabrina,
Smith Steven P.,
Jia Zongchao
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110001375
Subject(s) - cellulosome , clostridium thermocellum , cohesin , heterotrimeric g protein , protein subunit , cellulase , chemistry , biochemistry , microbiology and biotechnology , crystallography , biology , dna , g protein , enzyme , chromatin , gene , signal transduction
The multimodular scaffoldin subunit CipA is the central component of the cellulosome, a multienzyme plant cell‐wall‐degrading complex, from Clostridium thermocellum . It captures secreted cellulases and hemicellulases and anchors the entire complex to the cell surface via high‐affinity calcium‐dependent interactions between cohesin and dockerin modules termed type I and type II interactions. The crystallization of a heterotrimeric complex comprising the type II cohesin module from the cell‐surface protein SdbA, a trimodular C‐terminal fragment of the scaffoldin CipA and the type I dockerin module from the CelD cellulase is reported. The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 119.37, b = 186.31, c = 191.17 Å. The crystals diffracted to 2.7 Å resolution with four or eight molecules of the ternary protein complex in the asymmetric unit.