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  • Title: Purification and crystallization of a multimodular heterotrimeric complex containing both type I and type II cohesin-dockerin interactions from the cellulosome of Clostridium thermocellum.
    Author: Currie MA, Adams JJ, Ali S, Smith SP, Jia Z.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 Mar 01; 66(Pt 3):327-9. PubMed ID: 20208173.
    Abstract:
    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 P2(1)2(1)2(1), with unit-cell parameters a = 119.37, b = 186.31, c = 191.17 A. The crystals diffracted to 2.7 A resolution with four or eight molecules of the ternary protein complex in the asymmetric unit.
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