Purification and Crystallization of a Multimodular Heterotrimeric Complex Containing Both Type I and Type II Cohesin-dockerin Interactions from the Cellulosome of Clostridium thermocellum
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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 119.37, b = 186.31, c = 191.17 {angstrom}. The crystals diffracted to 2.7 {angstrom} resolution with four or eight molecules of the ternary protein complex in the asymmetric unit.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE SC OFFICE OF SCIENCE (SC)
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1042200
- Report Number(s):
- BNL-97878-2012-JA; TRN: US201212%%611
- Journal Information:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, Issue 3
- Country of Publication:
- United States
- Language:
- English
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