| pubmed-article:11273698 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1516143 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11273698 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:11273698 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11273698 | pubmed:dateCreated | 2001-3-29 | lld:pubmed |
| pubmed-article:11273698 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:abstractText | The type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase into the bacterial cellulosome, a multienzyme cellulolytic complex, via its interaction with a receptor domain (cohesin domain) of the cellulosomal scaffolding subunit. The highly conserved dockerin domain is characterized by two Ca(2+)-binding sites with sequence similarity to the EF-hand motif. Here, we present the three-dimensional solution structure of the 69 residue dockerin domain of Clostridium thermocellum cellobiohydrolase CelS. Torsion angle dynamics calculations utilizing a total of 728 NOE-derived distance constraints and 79 torsion angle restraints yielded an ensemble of 20 structures with an average backbone r.m.s.d. for residues 5 to 29 and 32 to 66 of 0.54 A from the mean structure. The structure consists of two Ca(2+)-binding loop-helix motifs connected by a linker; the E helices entering each loop of the classical EF-hand motif are absent from the dockerin domain. Each dockerin Ca(2+)-binding subdomain is stabilized by a cluster of buried hydrophobic side-chains. Structural comparisons reveal that, in its non-complexed state, the dockerin fold displays a dramatic departure from that of Ca(2+)-bound EF-hand domains. A putative cohesin-binding surface, comprised of conserved hydrophobic and basic residues, is proposed, providing new insight into cellulosome assembly. | lld:pubmed |
| pubmed-article:11273698 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11273698 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11273698 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11273698 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11273698 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:11273698 | pubmed:author | pubmed-author:WestlerW MWM | lld:pubmed |
| pubmed-article:11273698 | pubmed:author | pubmed-author:WuJ HJH | lld:pubmed |
| pubmed-article:11273698 | pubmed:author | pubmed-author:VolkmanB FBF | lld:pubmed |
| pubmed-article:11273698 | pubmed:author | pubmed-author:LytleB LBL | lld:pubmed |
| pubmed-article:11273698 | pubmed:author | pubmed-author:HeckmanM PMP | lld:pubmed |
| pubmed-article:11273698 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11273698 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11273698 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:11273698 | pubmed:volume | 307 | lld:pubmed |
| pubmed-article:11273698 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11273698 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11273698 | pubmed:pagination | 745-53 | lld:pubmed |
| pubmed-article:11273698 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11273698 | pubmed:meshHeading | pubmed-meshheading:11273698... | lld:pubmed |
| pubmed-article:11273698 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11273698 | pubmed:articleTitle | Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain. | lld:pubmed |
| pubmed-article:11273698 | pubmed:affiliation | Department of Chemical Engineering, University of Rochester, NY 14627-0166, USA. | lld:pubmed |
| pubmed-article:11273698 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11273698 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11273698 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11273698 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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