| pubmed-article:10867237 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10867237 | lifeskim:mentions | umls-concept:C0038409 | lld:lifeskim |
| pubmed-article:10867237 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:10867237 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:10867237 | lifeskim:mentions | umls-concept:C0119452 | lld:lifeskim |
| pubmed-article:10867237 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10867237 | pubmed:dateCreated | 2000-9-8 | lld:pubmed |
| pubmed-article:10867237 | pubmed:abstractText | Glucosyltransferases (GtfB/C/D) of Streptococcus mutans, a pathogen for human dental caries, synthesize water-insoluble glucan through the hydrolysis of sucrose. Genetic and biochemical approaches have identified several active sites of these enzymes, but no three-dimensional (3D) structural evidence is yet available to elucidate the subdomain arrangement and molecular mechanism of catalysis. Based on a combined sequence and secondary structure alignment against known crystal structures of segments from closely related proteins, we propose here the 3D model of an N-terminal domain essential for the sucrose binding and splitting in GtfB. A Tim-barrel of (alpha/beta)(8) structural characteristics is revealed and the structural correlation for two peptides is described. | lld:pubmed |
| pubmed-article:10867237 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10867237 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10867237 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10867237 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10867237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10867237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10867237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10867237 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10867237 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10867237 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:ShiauY YYY | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:SASAKK | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:ChouH CHC | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:OldsB ABA | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:ChiaJ SJS | lld:pubmed |
| pubmed-article:10867237 | pubmed:author | pubmed-author:LowK FKF | lld:pubmed |
| pubmed-article:10867237 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10867237 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10867237 | pubmed:volume | 188 | lld:pubmed |
| pubmed-article:10867237 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10867237 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10867237 | pubmed:pagination | 75-9 | lld:pubmed |
| pubmed-article:10867237 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:meshHeading | pubmed-meshheading:10867237... | lld:pubmed |
| pubmed-article:10867237 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10867237 | pubmed:articleTitle | Three-dimensional modelling of the catalytic domain of Streptococcus mutans glucosyltransferase GtfB. | lld:pubmed |
| pubmed-article:10867237 | pubmed:affiliation | Graduate Institute of Oral Biology, College of Medicine, National Taiwan University, Taipei. | lld:pubmed |
| pubmed-article:10867237 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10867237 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10867237 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10867237 | lld:pubmed |
