FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2019596708> ?p ?o ?g. }

• W2019596708 endingPage "309" @default.
• W2019596708 startingPage "289" @default.
• W2019596708 abstract "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 Å resolution and refined to a final crystallographic R-factor of 17.5% using data from 8 to 2.2 Å 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 β-sheet flanked on one side by two α-helices and on the other side by an irregular segment containing three short 310-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." @default.
• W2019596708 created "2016-06-24" @default.
• W2019596708 creator A5002741354 @default.
• W2019596708 creator A5018745563 @default.
• W2019596708 creator A5026938014 @default.
• W2019596708 creator A5028219744 @default.
• W2019596708 creator A5051914439 @default.
• W2019596708 creator A5052742336 @default.
• W2019596708 creator A5056520004 @default.
• W2019596708 creator A5061896741 @default.
• W2019596708 creator A5063495689 @default.
• W2019596708 creator A5075149377 @default.
• W2019596708 creator A5078652050 @default.
• W2019596708 date "1996-01-01" @default.
• W2019596708 modified "2023-10-16" @default.
• W2019596708 title "Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 Å resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture" @default.
• W2019596708 cites W1486158855 @default.
• W2019596708 cites W1489526459 @default.
• W2019596708 cites W1490514916 @default.
• W2019596708 cites W1536923222 @default.
• W2019596708 cites W1538959211 @default.
• W2019596708 cites W1546896179 @default.
• W2019596708 cites W1547383512 @default.
• W2019596708 cites W1557525759 @default.
• W2019596708 cites W1572376186 @default.
• W2019596708 cites W1605429854 @default.
• W2019596708 cites W172254742 @default.
• W2019596708 cites W1792325685 @default.
• W2019596708 cites W1873199501 @default.
• W2019596708 cites W1902072415 @default.
• W2019596708 cites W1906830706 @default.
• W2019596708 cites W1967604761 @default.
• W2019596708 cites W1969419384 @default.
• W2019596708 cites W1975993749 @default.
• W2019596708 cites W1977953918 @default.
• W2019596708 cites W1980056644 @default.
• W2019596708 cites W1982180350 @default.
• W2019596708 cites W1985550864 @default.
• W2019596708 cites W1986191025 @default.
• W2019596708 cites W1990724346 @default.
• W2019596708 cites W1996607909 @default.
• W2019596708 cites W1996788540 @default.
• W2019596708 cites W1999068901 @default.
• W2019596708 cites W2008708467 @default.
• W2019596708 cites W2010060878 @default.
• W2019596708 cites W2010909615 @default.
• W2019596708 cites W2014694459 @default.
• W2019596708 cites W2019717176 @default.
• W2019596708 cites W2028231353 @default.
• W2019596708 cites W2033643793 @default.
• W2019596708 cites W2042280550 @default.
• W2019596708 cites W2042987185 @default.
• W2019596708 cites W2043652214 @default.
• W2019596708 cites W2049465363 @default.
• W2019596708 cites W2050129721 @default.
• W2019596708 cites W2058639125 @default.
• W2019596708 cites W2060305056 @default.
• W2019596708 cites W2064035407 @default.
• W2019596708 cites W2065825921 @default.
• W2019596708 cites W2067645788 @default.
• W2019596708 cites W2069775699 @default.
• W2019596708 cites W2072594030 @default.
• W2019596708 cites W2075356247 @default.
• W2019596708 cites W2078057889 @default.
• W2019596708 cites W2078136648 @default.
• W2019596708 cites W2079178286 @default.
• W2019596708 cites W2079351920 @default.
• W2019596708 cites W2082116200 @default.
• W2019596708 cites W2082488805 @default.
• W2019596708 cites W2084228126 @default.
• W2019596708 cites W2084585743 @default.
• W2019596708 cites W2085634727 @default.
• W2019596708 cites W2085825530 @default.
• W2019596708 cites W2088644658 @default.
• W2019596708 cites W2089952662 @default.
• W2019596708 cites W2090208114 @default.
• W2019596708 cites W2094089338 @default.
• W2019596708 cites W2097925228 @default.
• W2019596708 cites W2098401999 @default.
• W2019596708 cites W2109311175 @default.
• W2019596708 cites W2116275717 @default.
• W2019596708 cites W2122646497 @default.
• W2019596708 cites W2139754659 @default.
• W2019596708 cites W2154011403 @default.
• W2019596708 cites W2226952709 @default.
• W2019596708 cites W2344114075 @default.
• W2019596708 cites W337892304 @default.
• W2019596708 cites W33811216 @default.
• W2019596708 cites W4229676100 @default.
• W2019596708 doi "https://doi.org/10.1006/jmbi.1996.0024" @default.
• W2019596708 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8551521" @default.
• W2019596708 hasPublicationYear "1996" @default.
• W2019596708 type Work @default.
• W2019596708 sameAs 2019596708 @default.
• W2019596708 citedByCount "200" @default.
• W2019596708 countsByYear W20195967082012 @default.
• W2019596708 countsByYear W20195967082013 @default.
• W2019596708 countsByYear W20195967082014 @default.

• next