| pubmed-article:16384918 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C1314972 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0237497 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0185023 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C1947904 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C1999228 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C2825781 | lld:lifeskim |
| pubmed-article:16384918 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16384918 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16384918 | pubmed:dateCreated | 2006-1-12 | lld:pubmed |
| pubmed-article:16384918 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16384918 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:16384918 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16384918 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16384918 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16384918 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16384918 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16384918 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16384918 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16384918 | pubmed:author | pubmed-author:GeisD RDR | lld:pubmed |
| pubmed-article:16384918 | pubmed:author | pubmed-author:JiaZongchaoZ | lld:pubmed |
| pubmed-article:16384918 | pubmed:author | pubmed-author:SmithSteven... | lld:pubmed |
| pubmed-article:16384918 | pubmed:author | pubmed-author:AdamsJarrett... | lld:pubmed |
| pubmed-article:16384918 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16384918 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:16384918 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16384918 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16384918 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16384918 | pubmed:pagination | 305-10 | lld:pubmed |
| pubmed-article:16384918 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
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| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:meshHeading | pubmed-meshheading:16384918... | lld:pubmed |
| pubmed-article:16384918 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16384918 | pubmed:articleTitle | Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex. | lld:pubmed |
| pubmed-article:16384918 | pubmed:affiliation | Department of Biochemistry and Protein Function Discovery Group, Queen's University, Kingston, ON, Canada K7L 3N6. | lld:pubmed |
| pubmed-article:16384918 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16384918 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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