Structural insights into omega-class glutathione transferases: a snapshot of enzyme reduction and identification of a non-catalytic ligandin site
Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl...
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| description | Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl)glutathiones to acetophenones. Both types of reaction result in the formation of a mixed-disulfide of the enzyme with glutathione through the catalytic cysteine (C32). Recycling of the enzyme utilizes a second glutathione molecule and results in oxidized glutathione (GSSG) release. The crystal structure of an active-site mutant (C32A) of the hGSTO1-1 isozyme in complex with GSSG provides a snapshot of the enzyme in the process of regeneration. GSSG occupies both the G (GSH-binding) and H (hydrophobic-binding) sites and causes re-arrangement of some H-site residues. In the same structure we demonstrate the existence of a novel "ligandin" binding site deep within in the dimer interface of this enzyme, containing S-(4-nitrophenacyl)glutathione, an isozyme-specific substrate for hGSTO1-1. The ligandin site, conserved in Omega class GSTs from a range of species, is hydrophobic in nature and may represent the binding location for tocopherol esters that are uncompetitive hGSTO1-1 inhibitors. |
| doi_str_mv | 10.1371/journal.pone.0060324 |
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The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl)glutathiones to acetophenones. Both types of reaction result in the formation of a mixed-disulfide of the enzyme with glutathione through the catalytic cysteine (C32). Recycling of the enzyme utilizes a second glutathione molecule and results in oxidized glutathione (GSSG) release. The crystal structure of an active-site mutant (C32A) of the hGSTO1-1 isozyme in complex with GSSG provides a snapshot of the enzyme in the process of regeneration. GSSG occupies both the G (GSH-binding) and H (hydrophobic-binding) sites and causes re-arrangement of some H-site residues. In the same structure we demonstrate the existence of a novel "ligandin" binding site deep within in the dimer interface of this enzyme, containing S-(4-nitrophenacyl)glutathione, an isozyme-specific substrate for hGSTO1-1. The ligandin site, conserved in Omega class GSTs from a range of species, is hydrophobic in nature and may represent the binding location for tocopherol esters that are uncompetitive hGSTO1-1 inhibitors.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0060324</identifier><identifier>PMID: 23593192</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Binding Sites ; BIO ; Biology ; Catalysis ; Chemistry ; Crystal structure ; Cysteine ; Electrons ; Enzymes ; Esters ; Glutathione ; Glutathione Transferase - chemistry ; Glutathione Transferase - metabolism ; Humans ; Hydrophobicity ; Ligands ; Models, Molecular ; Molecular Docking Simulation ; Molecular Sequence Data ; Protein Conformation ; Protein Multimerization ; Proteins ; Reduction ; Regeneration ; Sequence Alignment ; Substrates ; Thiols ; Tocopherol ; Tocopherols ; Transferases</subject><ispartof>PloS one, 2013-04, Vol.8 (4), p.e60324-e60324</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Brock et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl)glutathiones to acetophenones. Both types of reaction result in the formation of a mixed-disulfide of the enzyme with glutathione through the catalytic cysteine (C32). Recycling of the enzyme utilizes a second glutathione molecule and results in oxidized glutathione (GSSG) release. The crystal structure of an active-site mutant (C32A) of the hGSTO1-1 isozyme in complex with GSSG provides a snapshot of the enzyme in the process of regeneration. GSSG occupies both the G (GSH-binding) and H (hydrophobic-binding) sites and causes re-arrangement of some H-site residues. 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The ligandin site, conserved in Omega class GSTs from a range of species, is hydrophobic in nature and may represent the binding location for tocopherol esters that are uncompetitive hGSTO1-1 inhibitors.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>BIO</subject><subject>Biology</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>Crystal structure</subject><subject>Cysteine</subject><subject>Electrons</subject><subject>Enzymes</subject><subject>Esters</subject><subject>Glutathione</subject><subject>Glutathione Transferase - chemistry</subject><subject>Glutathione Transferase - metabolism</subject><subject>Humans</subject><subject>Hydrophobicity</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Docking Simulation</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein 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One</addtitle><date>2013-04-09</date><risdate>2013</risdate><volume>8</volume><issue>4</issue><spage>e60324</spage><epage>e60324</epage><pages>e60324-e60324</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Glutathione transferases (GSTs) are dimeric enzymes containing one active-site per monomer. The omega-class GSTs (hGSTO1-1 and hGSTO2-2 in humans) are homodimeric and carry out a range of reactions including the glutathione-dependant reduction of a range of compounds and the reduction of S-(phenacyl)glutathiones to acetophenones. Both types of reaction result in the formation of a mixed-disulfide of the enzyme with glutathione through the catalytic cysteine (C32). Recycling of the enzyme utilizes a second glutathione molecule and results in oxidized glutathione (GSSG) release. The crystal structure of an active-site mutant (C32A) of the hGSTO1-1 isozyme in complex with GSSG provides a snapshot of the enzyme in the process of regeneration. GSSG occupies both the G (GSH-binding) and H (hydrophobic-binding) sites and causes re-arrangement of some H-site residues. In the same structure we demonstrate the existence of a novel "ligandin" binding site deep within in the dimer interface of this enzyme, containing S-(4-nitrophenacyl)glutathione, an isozyme-specific substrate for hGSTO1-1. The ligandin site, conserved in Omega class GSTs from a range of species, is hydrophobic in nature and may represent the binding location for tocopherol esters that are uncompetitive hGSTO1-1 inhibitors.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23593192</pmid><doi>10.1371/journal.pone.0060324</doi><tpages>e60324</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Binding Sites BIO Biology Catalysis Chemistry Crystal structure Cysteine Electrons Enzymes Esters Glutathione Glutathione Transferase - chemistry Glutathione Transferase - metabolism Humans Hydrophobicity Ligands Models, Molecular Molecular Docking Simulation Molecular Sequence Data Protein Conformation Protein Multimerization Proteins Reduction Regeneration Sequence Alignment Substrates Thiols Tocopherol Tocopherols Transferases |
| title | Structural insights into omega-class glutathione transferases: a snapshot of enzyme reduction and identification of a non-catalytic ligandin site |
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