2b59
From Proteopedia
(New page: 200px<br /><applet load="2b59" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b59, resolution 2.11Å" /> '''The type II cohesin ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size=" | + | [[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b59, resolution 2.11Å" /> | caption="2b59, resolution 2.11Å" /> | ||
'''The type II cohesin dockerin complex'''<br /> | '''The type II cohesin dockerin complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial cell-surface attachment of macromolecular complexes maintains | + | 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== | ==About this Structure== | ||
| - | 2B59 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] and [http://en.wikipedia.org/wiki/Clostridium_thermocellum_atcc_27405 Clostridium thermocellum atcc 27405] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2B59 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] and [http://en.wikipedia.org/wiki/Clostridium_thermocellum_atcc_27405 Clostridium thermocellum atcc 27405] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Clostridium thermocellum atcc 27405]] | [[Category: Clostridium thermocellum atcc 27405]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Adams, J | + | [[Category: Adams, J J.]] |
| - | [[Category: BSGI, Montreal-Kingston | + | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] |
| - | [[Category: Smith, S | + | [[Category: Smith, S P.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
| Line 25: | Line 25: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:18 2008'' |
Revision as of 14:34, 21 February 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 with as ligand. 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 Thu Feb 21 16:34:18 2008
Categories: Clostridium thermocellum | Clostridium thermocellum atcc 27405 | Protein complex | Adams, J J. | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Smith, S P. | CA | Bsgi | Cellulosome | Ef hand | Montreal-kingston bacterial structural genomics initiative | Protein-protein complex | Structural genomics
