| pubmed-article:15667212 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0041258 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:15667212 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:15667212 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15667212 | pubmed:dateCreated | 2005-1-25 | lld:pubmed |
| pubmed-article:15667212 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:abstractText | When the tryptophan synthase alpha- and beta(2)-subunits combine to form the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is stimulated by 1-2 orders of magnitude. To elucidate the structural basis of this mutual activation, it is necessary to determine the structures of the alpha- and beta-subunits alone and together with the alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase alpha(2)beta(2)-complex from Salmonella typhimurium (Stalpha(2)beta(2)-complex) have already been reported. However, the structures of the subunit alone from mesophiles have not yet been determined. The structure of the tryptophan synthase alpha-subunit alone from Escherichia coli (Ecalpha-subunit) was determined by an X-ray crystallographic analysis at 2.3 A, which is the first report on the subunits alone from the mesophiles. The biggest difference between the structures of the Ecalpha-subunit alone and the alpha-subunit in the Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in the Stalpha-subunit, including an active site residue (Asp60), was changed to a flexible loop in the Ecalpha-subunit alone. The conversion of the helix to a loop resulted in the collapse of the correct active site conformation. This region is also an important part for the mutual activation in the Stalpha(2)beta(2)-complex and interaction with the beta-subunit. These results suggest that the formation of helix 2'that is essential for the stimulation of the enzymatic activity of the alpha-subunit is constructed by the induced-fit mode involved in conformational changes upon interaction between the alpha- and beta-subunits. This also confirms the prediction of the conformational changes based on the thermodynamic analysis for the association between the alpha- and beta-subunits. | lld:pubmed |
| pubmed-article:15667212 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15667212 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15667212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15667212 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15667212 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15667212 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:MorimotoYukio... | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:TsukiharaTomi... | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:OgasaharaKyok... | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:YutaniKatsuhi... | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:NishioKazuyaK | lld:pubmed |
| pubmed-article:15667212 | pubmed:author | pubmed-author:IshizukaManab... | lld:pubmed |
| pubmed-article:15667212 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15667212 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15667212 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:15667212 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15667212 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15667212 | pubmed:pagination | 1184-92 | lld:pubmed |
| pubmed-article:15667212 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:meshHeading | pubmed-meshheading:15667212... | lld:pubmed |
| pubmed-article:15667212 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15667212 | pubmed:articleTitle | Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. | lld:pubmed |
| pubmed-article:15667212 | pubmed:affiliation | Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. | lld:pubmed |
| pubmed-article:15667212 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15667212 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15667212 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:946204 | entrezgene:pubmed | pubmed-article:15667212 | lld:entrezgene |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15667212 | lld:pubmed |
