2b59: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2b59" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b59, resolution 2.11Å" /> '''The type II cohesin ...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2b59, resolution 2.11&Aring;" />
caption="2b59, resolution 2.11&Aring;" />
'''The type II cohesin dockerin complex'''<br />
'''The type II cohesin dockerin complex'''<br />


==Overview==
==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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA].  
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.J.]]
[[Category: Adams, J J.]]
[[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: CA]]
[[Category: CA]]
[[Category: bsgi]]
[[Category: bsgi]]
Line 25: Line 25:
[[Category: structural genomics]]
[[Category: structural genomics]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:34:07 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:18 2008''