| pubmed-article:2184433 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0021237 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:2184433 | lifeskim:mentions | umls-concept:C0377355 | lld:lifeskim |
| pubmed-article:2184433 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2184433 | pubmed:dateCreated | 1990-5-25 | lld:pubmed |
| pubmed-article:2184433 | pubmed:abstractText | The recombinant synthase domain of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli has been crystallized, and the structure has been solved at 4 A resolution. Two closely related crystal forms grown from ammonium sulphate diffract to 2 A resolution. One form (space group R32, a = 163 A, alpha = 29.5 degrees) contains the unliganded synthase domain; the second crystal form (space group P6(3)22, a = 144 A, c = 158 A) is co-crystallized with the substrate analogue N-(5'-phosphoribit-1-yl)anthranilate. The structure of the synthase-inhibitor complex has been solved by the molecular replacement method. This achievement represents the first successful use of a (beta alpha)8-barrel monomer as a trial model. The recombinant synthase domain associates as a trimer in the crystal, the molecules being related by a pseudo-crystallographic triad. The interface contacts between the three domains are mediated by those residues that are also involved in the domain interface of the bifunctional enzyme. This system provides a model for an interface which is used in both intermolecular and intramolecular domain contacts. | lld:pubmed |
| pubmed-article:2184433 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2184433 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2184433 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2184433 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2184433 | pubmed:issn | 0269-2139 | lld:pubmed |
| pubmed-article:2184433 | pubmed:author | pubmed-author:FooGG | lld:pubmed |
| pubmed-article:2184433 | pubmed:author | pubmed-author:JansoniusJ... | lld:pubmed |
| pubmed-article:2184433 | pubmed:author | pubmed-author:WilmannsMM | lld:pubmed |
| pubmed-article:2184433 | pubmed:author | pubmed-author:SchlagenhaufE... | lld:pubmed |
| pubmed-article:2184433 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2184433 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:2184433 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2184433 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2184433 | pubmed:pagination | 173-80 | lld:pubmed |
| pubmed-article:2184433 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:meshHeading | pubmed-meshheading:2184433-... | lld:pubmed |
| pubmed-article:2184433 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2184433 | pubmed:articleTitle | Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue. | lld:pubmed |
| pubmed-article:2184433 | pubmed:affiliation | Department of Structural Biology, University of Basel, Switzerland. | lld:pubmed |
| pubmed-article:2184433 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2184433 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2184433 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:2839_218... | literatureCitation:pubmed | pubmed-article:2184433 | lld:drugbank |
| entrez-gene:945519 | entrezgene:pubmed | pubmed-article:2184433 | lld:entrezgene |
