2b59: Difference between revisions
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[[Image:2b59.gif|left|200px]] | [[Image:2b59.gif|left|200px]] | ||
'''The type II cohesin dockerin complex''' | {{Structure | ||
|PDB= 2b59 |SIZE=350|CAPTION= <scene name='initialview01'>2b59</scene>, resolution 2.11Å | |||
|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 [ | 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:// | 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 | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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, resolution 2.11Å | |||||||
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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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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 genomic