The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins
Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the pr...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2008-09, Vol.477 (1), p.98-104 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Smeets, Aude Marchand, Cécile Linard, Dominique Knoops, Bernard Declercq, Jean-Paul |
| description | Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed. |
| doi_str_mv | 10.1016/j.abb.2008.04.036 |
| format | Article |
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PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2008.04.036</identifier><identifier>PMID: 18489898</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Antioxidant enzyme ; Benzoate ligand ; Biopolymers - chemistry ; Biopolymers - metabolism ; Blotting, Western ; Crystallography, X-Ray ; Disulfides - chemistry ; Human peroxiredoxin ; Humans ; Models, Molecular ; Oxidation-Reduction ; Oxidized state ; Peroxiredoxins - chemistry ; Peroxiredoxins - metabolism ; Protein Conformation ; Sulfenic acid ; Thioredoxin fold ; Thioredoxin peroxidase ; X-ray crystal structure</subject><ispartof>Archives of biochemistry and biophysics, 2008-09, Vol.477 (1), p.98-104</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-6adc9324aef9299e33e0eacf8eba7852e78d81a4444ef2565a5a5c4ab83571583</citedby><cites>FETCH-LOGICAL-c351t-6adc9324aef9299e33e0eacf8eba7852e78d81a4444ef2565a5a5c4ab83571583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2008.04.036$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18489898$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smeets, Aude</creatorcontrib><creatorcontrib>Marchand, Cécile</creatorcontrib><creatorcontrib>Linard, Dominique</creatorcontrib><creatorcontrib>Knoops, Bernard</creatorcontrib><creatorcontrib>Declercq, Jean-Paul</creatorcontrib><title>The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed.</description><subject>Antioxidant enzyme</subject><subject>Benzoate ligand</subject><subject>Biopolymers - chemistry</subject><subject>Biopolymers - metabolism</subject><subject>Blotting, Western</subject><subject>Crystallography, X-Ray</subject><subject>Disulfides - chemistry</subject><subject>Human peroxiredoxin</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Oxidation-Reduction</subject><subject>Oxidized state</subject><subject>Peroxiredoxins - chemistry</subject><subject>Peroxiredoxins - metabolism</subject><subject>Protein Conformation</subject><subject>Sulfenic acid</subject><subject>Thioredoxin fold</subject><subject>Thioredoxin peroxidase</subject><subject>X-ray crystal structure</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UcuuFCEQJUbjHa9-gBvDyl23PLp76LgyE1_JTdxc14SGIsOkgRZote9n-YUyziTGjVRCJcWpc6o4CL2kpKWEDm9OrZqmlhEiWtK1hA-P0I6ScWgIF91jtCOE8GYUA71Bz3I-EUJpN7Cn6IaKTow1dujX_RGwTlsuasa5pFWXNUHG0eL40xn3AAbbmPyfynH1KuAFUn1KYOodcI9_uHLEte5CScrHGfQ6q4SNy-tsnQE8xWCwjsG65HGpekuKS8yVGcLD5lVxGnvQRxVc9mc1rMq2OF0nYs1hy_8q5ufoiVVzhhfXfIu-fnh_f_jU3H35-Pnw7q7RvKelGZTRI2edAjuycQTOgYDSVsCk9qJnsBdGUNXVA5b1Q69q6E5Ngvd72gt-i15feOu431bIRXqXNcyzChDXLIexY4wOZyC9AHWKOSewcknOq7RJSuTZKHmS1Sh5NkqSTlajas-rK_k6eTB_O67OVMDbCwDqit8dJJm1g6DB1I_QRZro_kP_G-GoqRo</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Smeets, Aude</creator><creator>Marchand, Cécile</creator><creator>Linard, Dominique</creator><creator>Knoops, Bernard</creator><creator>Declercq, Jean-Paul</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins</title><author>Smeets, Aude ; Marchand, Cécile ; Linard, Dominique ; Knoops, Bernard ; Declercq, Jean-Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-6adc9324aef9299e33e0eacf8eba7852e78d81a4444ef2565a5a5c4ab83571583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Antioxidant enzyme</topic><topic>Benzoate ligand</topic><topic>Biopolymers - chemistry</topic><topic>Biopolymers - metabolism</topic><topic>Blotting, Western</topic><topic>Crystallography, X-Ray</topic><topic>Disulfides - chemistry</topic><topic>Human peroxiredoxin</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Oxidation-Reduction</topic><topic>Oxidized state</topic><topic>Peroxiredoxins - chemistry</topic><topic>Peroxiredoxins - metabolism</topic><topic>Protein Conformation</topic><topic>Sulfenic acid</topic><topic>Thioredoxin fold</topic><topic>Thioredoxin peroxidase</topic><topic>X-ray crystal structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smeets, Aude</creatorcontrib><creatorcontrib>Marchand, Cécile</creatorcontrib><creatorcontrib>Linard, Dominique</creatorcontrib><creatorcontrib>Knoops, Bernard</creatorcontrib><creatorcontrib>Declercq, Jean-Paul</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smeets, Aude</au><au>Marchand, Cécile</au><au>Linard, Dominique</au><au>Knoops, Bernard</au><au>Declercq, Jean-Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2008-09-01</date><risdate>2008</risdate><volume>477</volume><issue>1</issue><spage>98</spage><epage>104</epage><pages>98-104</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18489898</pmid><doi>10.1016/j.abb.2008.04.036</doi><tpages>7</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 2008-09, Vol.477 (1), p.98-104 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Antioxidant enzyme Benzoate ligand Biopolymers - chemistry Biopolymers - metabolism Blotting, Western Crystallography, X-Ray Disulfides - chemistry Human peroxiredoxin Humans Models, Molecular Oxidation-Reduction Oxidized state Peroxiredoxins - chemistry Peroxiredoxins - metabolism Protein Conformation Sulfenic acid Thioredoxin fold Thioredoxin peroxidase X-ray crystal structure |
| title | The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins |
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