| pubmed-article:15784255 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15784255 | lifeskim:mentions | umls-concept:C0544157 | lld:lifeskim |
| pubmed-article:15784255 | lifeskim:mentions | umls-concept:C0012611 | lld:lifeskim |
| pubmed-article:15784255 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15784255 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:15784255 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15784255 | pubmed:dateCreated | 2005-3-23 | lld:pubmed |
| pubmed-article:15784255 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:abstractText | Trehalose (alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranose) is a non-reducing diglucoside found in various organisms that serves as a carbohydrate reserve and as an agent that protects against a variety of physical and chemical stresses. Deinococcus radiodurans possesses an alternative biosynthesis pathway for the synthesis of trehalose from maltooligosaccharides. This reaction is mediated by two enzymes: maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase). Here, we present the 1.1A resolution crystal structure of MTHase. It consists of three major domains: two beta-sheet domains and a conserved glycosidase (beta/alpha)8 barrel catalytic domain. Three subdomains consisting of short insertions were identified within the catalytic domain. Subsequently, structures of MTHase in complex with maltose and trehalose were obtained at 1.2 A and 1.5 A resolution, respectively. These structures reveal the importance of the three inserted subdomains in providing the key residues required for substrate recognition. Trehalose is recognised specifically in the +1 and +2 binding subsites by an extensive hydrogen-bonding network and a strong hydrophobic stacking interaction in between two aromatic residues. Moreover, upon binding to maltose, which mimics the substrate sugar chain, a major concerted conformational change traps the sugar chain in the active site. The presence of magnesium in the active site of the MTHase-maltose complex suggests that MTHase activity may be regulated by divalent cations. | lld:pubmed |
| pubmed-article:15784255 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15784255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15784255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15784255 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15784255 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15784255 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15784255 | pubmed:author | pubmed-author:LeirosIngarI | lld:pubmed |
| pubmed-article:15784255 | pubmed:author | pubmed-author:McSweeneySean... | lld:pubmed |
| pubmed-article:15784255 | pubmed:author | pubmed-author:LeonardGordon... | lld:pubmed |
| pubmed-article:15784255 | pubmed:author | pubmed-author:TimminsJoanna... | lld:pubmed |
| pubmed-article:15784255 | pubmed:author | pubmed-author:LeirosHanna-K... | lld:pubmed |
| pubmed-article:15784255 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15784255 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15784255 | pubmed:volume | 347 | lld:pubmed |
| pubmed-article:15784255 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15784255 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15784255 | pubmed:pagination | 949-63 | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:meshHeading | pubmed-meshheading:15784255... | lld:pubmed |
| pubmed-article:15784255 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15784255 | pubmed:articleTitle | Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides. | lld:pubmed |
| pubmed-article:15784255 | pubmed:affiliation | Macromolecular Crystallography Group, European Synchrotron Radiation Facility, B.P. 220, 6 rue Jules Horowitz, F-38043 Grenoble Cedex, France. | lld:pubmed |
| pubmed-article:15784255 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15784255 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15784255 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15784255 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15784255 | lld:pubmed |
