1e6b: Difference between revisions
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==Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana== | ==Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana== | ||
<StructureSection load='1e6b' size='340' side='right' caption='[[1e6b]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1e6b' size='340' side='right'caption='[[1e6b]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E6B FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E6B FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e6b_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e6b_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Lapthorn, A J]] | [[Category: Lapthorn, A J]] | ||
[[Category: Thom, R]] | [[Category: Thom, R]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 09:33, 12 June 2019
Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thalianaCrystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana
Structural highlights
Function[GSTZ1_ARATH] Acts a maleylacetone isomerase. Also catalyzes the glutathione-dependent dehalogenation of dichloroacetic acid to glyoxylic acid. In vitro, possesses glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe cis-trans isomerisation of maleylacetoacetate to fumarylacetoacetate is the penultimate step in the tyrosine/phenylalanine catabolic pathway and has recently been shown to be catalysed by glutathione S-transferase enzymes belonging to the zeta class. Given this primary metabolic role it is unsurprising that zeta class glutathione S-transferases are well conserved over a considerable period of evolution, being found in vertebrates, plants, insects and fungi. The structure of this glutathione S-transferase, cloned from Arabidopsis thaliana, has been solved by single isomorphous replacement with anomalous scattering and refined to a final crystallographic R-factor of 19.6% using data from 25.0 A to 1.65 A. The zeta class enzyme adopts the canonical glutathione S-transferase fold and forms a homodimer with each subunit consisting of 221 residues. In agreement with structures of glutathione S-transferases from the theta and phi classes, a serine residue (Ser17) is present in the active site, at a position that would allow it to stabilise the thiolate anion of glutathione. Site-directed mutagenesis of this residue confirms its importance in catalysis. In addition, the role of a highly conserved cysteine residue (Cys19) present in the active site of the zeta class glutathione S-transferase enzymes is discussed. The structure of a zeta class glutathione S-transferase from Arabidopsis thaliana: characterisation of a GST with novel active-site architecture and a putative role in tyrosine catabolism.,Thom R, Dixon DP, Edwards R, Cole DJ, Lapthorn AJ J Mol Biol. 2001 May 18;308(5):949-62. PMID:11352584[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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