2b59
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2b59.gif|left|200px]] | [[Image:2b59.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2b59", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2b59| PDB=2b59 | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''The type II cohesin dockerin complex''' | '''The type II cohesin dockerin complex''' | ||
| Line 29: | Line 26: | ||
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | ||
[[Category: Smith, S P.]] | [[Category: Smith, S P.]] | ||
| - | [[Category: | + | [[Category: Bsgi]] |
| - | [[Category: | + | [[Category: Cellulosome]] |
| - | [[Category: | + | [[Category: Ef hand]] |
| - | [[Category: | + | [[Category: Montreal-kingston bacterial structural genomics initiative]] |
| - | [[Category: | + | [[Category: Protein-protein complex]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:52:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:52, 3 May 2008
The type II cohesin dockerin complex
Overview
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(a) = 1.44 x 10(10) M(-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.
About this Structure
2B59 is a Protein complex structure of sequences from Clostridium thermocellum and Clostridium thermocellum atcc 27405. Full crystallographic information is available from OCA.
Reference
Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex., Adams JJ, Pal G, Jia Z, Smith SP, Proc Natl Acad Sci U S A. 2006 Jan 10;103(2):305-10. Epub 2005 Dec 29. PMID:16384918 Page seeded by OCA on Sat May 3 19:52:20 2008
Categories: Clostridium thermocellum | Clostridium thermocellum atcc 27405 | Protein complex | Adams, J J. | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Smith, S P. | Bsgi | Cellulosome | Ef hand | Montreal-kingston bacterial structural genomics initiative | Protein-protein complex | Structural genomic
