2b59: Difference between revisions

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[[Image:2b59.gif|left|200px]]<br /><applet load="2b59" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2b59.gif|left|200px]]
caption="2b59, resolution 2.11&Aring;" />
 
'''The type II cohesin dockerin complex'''<br />
{{Structure
|PDB= 2b59 |SIZE=350|CAPTION= <scene name='initialview01'>2b59</scene>, resolution 2.11&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY=
|GENE= SdbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 Clostridium thermocellum ATCC 27405]), cipA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])
}}
 
'''The type II cohesin dockerin complex'''
 


==Overview==
==Overview==
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==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 <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].  
2B59 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B59 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16384918 16384918]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16384918 16384918]
[[Category: Clostridium thermocellum]]
[[Category: Clostridium thermocellum]]
[[Category: Clostridium thermocellum atcc 27405]]
[[Category: Clostridium thermocellum atcc 27405]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
[[Category: montreal-kingston bacterial structural genomics initiative]]
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
[[Category: structural genomics]]
[[Category: structural genomic]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:45 2008''

Revision as of 16:57, 20 March 2008

File:2b59.gif


PDB ID 2b59

Drag the structure with the mouse to rotate
, resolution 2.11Å
Ligands:
Gene: SdbA (Clostridium thermocellum ATCC 27405), cipA (Clostridium thermocellum)
Coordinates: save as pdb, mmCIF, xml



The type II cohesin dockerin complex


OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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