Mechanism of Bacterial Cell-Surface Attachment Revealed by the Structure of Cellulosomal Type II Cohesin-dockerin Complex
Journal Article
·
· Proceedings of the National Academy of Sciences of the USA
Bacterial cell-surface attachment of macromolecular complexes maintains the microorganism in close proximity to extracellular substrates and allows for optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant cell-wall polysaccharides. The mechanism of cellulosome retention to the bacterial cell surface involves a calcium-mediated protein-protein interaction between the dockerin (Doc) module from the cellulosomal scaffold and a cohesin (Coh) module of cell-surface proteins located within the proteoglycan layer. Here, we report the structure of an ultra-high-affinity (K{sub a} = 1.44 x 10{sup 10} M{sup 1-}) complex between type II Doc, together with its neighboring X module from the cellulosome scaffold of Clostridium thermocellum, and a type II Coh module associated with the bacterial cell surface. Identification of X module-Doc and X module-Coh contacts reveal roles for the X module in Doc stability and enhanced Coh recognition. This extremely tight interaction involves one face of the Coh and both helices of the Doc and comprises significant hydrophobic character and a complementary extensive hydrogen-bond network. This structure represents a unique mechanism for cell-surface attachment in anaerobic bacteria and provides a rationale for discriminating between type I and type II Coh modules.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 930123
- Report Number(s):
- BNL--80768-2008-JA
- Journal Information:
- Proceedings of the National Academy of Sciences of the USA, Journal Name: Proceedings of the National Academy of Sciences of the USA Vol. 103
- Country of Publication:
- United States
- Language:
- English
Similar Records
Probing the mechanism of cellulosome attachment to the Clostridium thermocellum cell surface: computer simulation of the Type II Cohesin-Dockerin complex and its variants
Purification and crystallization of a trimodular complex comprising the type II cohesin–dockerin interaction from the cellulosome of Clostridium thermocellum
Purification and Crystallization of a Multimodular Heterotrimeric Complex Containing Both Type I and Type II Cohesin-dockerin Interactions from the Cellulosome of Clostridium thermocellum
Journal Article
·
Fri Oct 01 00:00:00 EDT 2010
· Protein Engineering Design and Selection
·
OSTI ID:1017385
Purification and crystallization of a trimodular complex comprising the type II cohesin–dockerin interaction from the cellulosome of Clostridium thermocellum
Journal Article
·
Fri Dec 31 23:00:00 EST 2004
· Acta Crystallographica. Section F
·
OSTI ID:22356086
Purification and Crystallization of a Multimodular Heterotrimeric Complex Containing Both Type I and Type II Cohesin-dockerin Interactions from the Cellulosome of Clostridium thermocellum
Journal Article
·
Fri Dec 30 23:00:00 EST 2011
· Acta Crystallographica Section F: Structural Biology and Crystallization Communications
·
OSTI ID:1042200