| pubmed-article:8551521 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0017837 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C2825097 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0003737 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:8551521 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:8551521 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8551521 | pubmed:dateCreated | 1996-2-16 | lld:pubmed |
| pubmed-article:8551521 | pubmed:abstractText | Glutathione S-transferases (GST) are a family of multifunctional enzymes involved in the metabolization of a broad variety of xenobiotics and reactive endogenous compounds. The interest in plant glutathione S-transferases may be attributed to their agronomic value, since it has been demonstrated that glutathione conjugation for a variety of herbicides is the major resistance and selectivity factor in plants. The three-dimensional structure of glutathione S-transferase from the plant Arabidopsis thaliana has been solved by multiple isomorphous replacement and multiwavelength anomalous dispersion techniques at 3 A resolution and refined to a final crystallographic R-factor of 17.5% using data from 8 to 2.2 A resolution. The enzyme forms a dimer of two identical subunits each consisting of 211 residues. Each subunit is characterized by the GST-typical modular structure with two spatially distinct domains. Domain I consists of a central four-stranded beta-sheet flanked on one side by two alpha-helices and on the other side by an irregular segment containing three short 3(10)-helices, while domain II is entirely helical. The dimeric molecule is globular with a prominent large cavity formed between the two subunits. The active site is located in a cleft situated between domains I and II and each subunit binds two molecules of a competitive inhibitor S-hexylglutathione. Both hexyl moieties are oriented parallel and fill the H-subsite of the enzyme's active site. The glutathione peptide of one inhibitor, termed productive binding, occupies the G-subsite with multiple interactions similar to those observed for other glutathione S-transferases, while the glutathione backbone of the second inhibitor, termed unproductive binding, exhibits only weak interactions mediated by two polar contacts. A most striking difference from the mammalian glutathione S-transferases, which share a conserved catalytic tyrosine residue, is the lack of this tyrosine in the active site of the plant glutathione S-transferase. | lld:pubmed |
| pubmed-article:8551521 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8551521 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8551521 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8551521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8551521 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8551521 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:HuberRR | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:SchellJJ | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:PalmaWW | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:ZettlRR | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:HofPP | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:BartunikH DHD | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:ReinemerPP | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:BieselerBB | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:PradoFF | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:NeuefeindTT | lld:pubmed |
| pubmed-article:8551521 | pubmed:author | pubmed-author:KoellnII | lld:pubmed |
| pubmed-article:8551521 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8551521 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:8551521 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:8551521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8551521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8551521 | pubmed:pagination | 289-309 | lld:pubmed |
| pubmed-article:8551521 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
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| pubmed-article:8551521 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8551521 | pubmed:articleTitle | Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. | lld:pubmed |
| pubmed-article:8551521 | pubmed:affiliation | Bayer AG, GB Pflanzenschutz (PF-F Biotechnologie) Pflanzenschutzzentrum Monheim, Leverkusen, Germany. | lld:pubmed |
| pubmed-article:8551521 | pubmed:publicationType | Journal Article | lld:pubmed |
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