The structure and activity of the glutathione reductase from Streptococcus pneumoniae
The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxyge...
Gespeichert in:
| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2019-01, Vol.75 (1), p.54-61 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 61 |
|---|---|
| container_issue | 1 |
| container_start_page | 54 |
| container_title | Acta crystallographica. Section F, Structural biology communications |
| container_volume | 75 |
| creator | Sikanyika, Mwilye Aragão, David McDevitt, Christopher A. Maher, Megan J. |
| description | The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β‐sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 ± 24.7 µM) in comparison to other characterized GR enzymes.
The three‐dimensional crystal structure of the glutathione reductase from Streptococcus pneumoniae is reported at 2.56 Å resolution. |
| doi_str_mv | 10.1107/S2053230X18016527 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6317452</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2163012248</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4349-aec1c251e2ce1299ce4de205820f8d7ea1f6a71cee8487b5a702a466d64e38d13</originalsourceid><addsrcrecordid>eNqFkc9LHTEQx0OxVLH-AV5KwIuXZzNJNtm9FPRRa0HoQYV6CjE764vsbp75YXn_fXd5Vqw99DTDzOf7ZYYvIYfATgCY_nzFWSW4YD-hZqAqrt-RvXm0mGc7r_pdcpDSA2NsloFuPpBdwRSrgKs9cnO9QppyLC6XiNSOLbUu-yefNzR0NE_b-75km1c-jEgjthNpE9IuhoFe5YjrHFxwriS6HrEMYfQWP5L3ne0THjzXfXJz_vV6ebG4_PHt-_L0cuGkkM3CogPHK0DuEHjTOJQtTnfXnHV1q9FCp6wGh1jLWt9VVjNupVKtkijqFsQ--bL1XZe7AVuHY462N-voBxs3Jlhv_t6MfmXuw5NRArSs-GRw_GwQw2PBlM3gk8O-tyOGkgwHJRhwLusJPXqDPoQSx-m9meK6lozNhrClXAwpRexejgFm5gDMP7lNmk-vv3hR_ElpApot8Mv3uPm_ozm9PefLswpYI34D4XWkmA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2162784002</pqid></control><display><type>article</type><title>The structure and activity of the glutathione reductase from Streptococcus pneumoniae</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Sikanyika, Mwilye ; Aragão, David ; McDevitt, Christopher A. ; Maher, Megan J.</creator><creatorcontrib>Sikanyika, Mwilye ; Aragão, David ; McDevitt, Christopher A. ; Maher, Megan J.</creatorcontrib><description>The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β‐sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 ± 24.7 µM) in comparison to other characterized GR enzymes.
The three‐dimensional crystal structure of the glutathione reductase from Streptococcus pneumoniae is reported at 2.56 Å resolution.</description><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X18016527</identifier><identifier>PMID: 30605126</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; Biocatalysis ; Cloning, Molecular ; Crystal structure ; Crystallography, X-Ray ; Cytoplasm ; Detoxification ; Dimers ; Enzymes ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene Expression ; Genetic Vectors - chemistry ; Genetic Vectors - metabolism ; Glutathione ; Glutathione - chemistry ; Glutathione - metabolism ; Glutathione reductase ; Glutathione Reductase - chemistry ; Glutathione Reductase - genetics ; Glutathione Reductase - metabolism ; Intracellular ; Kinetics ; Models, Molecular ; Molecular structure ; NADP - chemistry ; NADP - metabolism ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Reactive nitrogen species ; Reactive oxygen species ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Research Communications ; Streptococcus infections ; Streptococcus pneumoniae ; Streptococcus pneumoniae - chemistry ; Streptococcus pneumoniae - enzymology ; Structural Homology, Protein ; Substrate Specificity ; X‐ray crystallography ; Zinc</subject><ispartof>Acta crystallographica. Section F, Structural biology communications, 2019-01, Vol.75 (1), p.54-61</ispartof><rights>International Union of Crystallography, 2019</rights><rights>Copyright Wiley Subscription Services, Inc. Jan 2019</rights><rights>International Union of Crystallography 2019 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4349-aec1c251e2ce1299ce4de205820f8d7ea1f6a71cee8487b5a702a466d64e38d13</citedby><cites>FETCH-LOGICAL-c4349-aec1c251e2ce1299ce4de205820f8d7ea1f6a71cee8487b5a702a466d64e38d13</cites><orcidid>0000-0003-1596-4841</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6317452/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6317452/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,27924,27925,45574,45575,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30605126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sikanyika, Mwilye</creatorcontrib><creatorcontrib>Aragão, David</creatorcontrib><creatorcontrib>McDevitt, Christopher A.</creatorcontrib><creatorcontrib>Maher, Megan J.</creatorcontrib><title>The structure and activity of the glutathione reductase from Streptococcus pneumoniae</title><title>Acta crystallographica. Section F, Structural biology communications</title><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><description>The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β‐sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 ± 24.7 µM) in comparison to other characterized GR enzymes.
The three‐dimensional crystal structure of the glutathione reductase from Streptococcus pneumoniae is reported at 2.56 Å resolution.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biocatalysis</subject><subject>Cloning, Molecular</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Cytoplasm</subject><subject>Detoxification</subject><subject>Dimers</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Gene Expression</subject><subject>Genetic Vectors - chemistry</subject><subject>Genetic Vectors - metabolism</subject><subject>Glutathione</subject><subject>Glutathione - chemistry</subject><subject>Glutathione - metabolism</subject><subject>Glutathione reductase</subject><subject>Glutathione Reductase - chemistry</subject><subject>Glutathione Reductase - genetics</subject><subject>Glutathione Reductase - metabolism</subject><subject>Intracellular</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>NADP - chemistry</subject><subject>NADP - metabolism</subject><subject>Protein Binding</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Conformation, beta-Strand</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Reactive nitrogen species</subject><subject>Reactive oxygen species</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Research Communications</subject><subject>Streptococcus infections</subject><subject>Streptococcus pneumoniae</subject><subject>Streptococcus pneumoniae - chemistry</subject><subject>Streptococcus pneumoniae - enzymology</subject><subject>Structural Homology, Protein</subject><subject>Substrate Specificity</subject><subject>X‐ray crystallography</subject><subject>Zinc</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9LHTEQx0OxVLH-AV5KwIuXZzNJNtm9FPRRa0HoQYV6CjE764vsbp75YXn_fXd5Vqw99DTDzOf7ZYYvIYfATgCY_nzFWSW4YD-hZqAqrt-RvXm0mGc7r_pdcpDSA2NsloFuPpBdwRSrgKs9cnO9QppyLC6XiNSOLbUu-yefNzR0NE_b-75km1c-jEgjthNpE9IuhoFe5YjrHFxwriS6HrEMYfQWP5L3ne0THjzXfXJz_vV6ebG4_PHt-_L0cuGkkM3CogPHK0DuEHjTOJQtTnfXnHV1q9FCp6wGh1jLWt9VVjNupVKtkijqFsQ--bL1XZe7AVuHY462N-voBxs3Jlhv_t6MfmXuw5NRArSs-GRw_GwQw2PBlM3gk8O-tyOGkgwHJRhwLusJPXqDPoQSx-m9meK6lozNhrClXAwpRexejgFm5gDMP7lNmk-vv3hR_ElpApot8Mv3uPm_ozm9PefLswpYI34D4XWkmA</recordid><startdate>201901</startdate><enddate>201901</enddate><creator>Sikanyika, Mwilye</creator><creator>Aragão, David</creator><creator>McDevitt, Christopher A.</creator><creator>Maher, Megan J.</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, 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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1596-4841</orcidid></search><sort><creationdate>201901</creationdate><title>The structure and activity of the glutathione reductase from Streptococcus pneumoniae</title><author>Sikanyika, Mwilye ; Aragão, David ; McDevitt, Christopher A. ; Maher, Megan J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4349-aec1c251e2ce1299ce4de205820f8d7ea1f6a71cee8487b5a702a466d64e38d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Biocatalysis</topic><topic>Cloning, Molecular</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Cytoplasm</topic><topic>Detoxification</topic><topic>Dimers</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Gene Expression</topic><topic>Genetic Vectors - chemistry</topic><topic>Genetic Vectors - metabolism</topic><topic>Glutathione</topic><topic>Glutathione - chemistry</topic><topic>Glutathione - metabolism</topic><topic>Glutathione reductase</topic><topic>Glutathione Reductase - chemistry</topic><topic>Glutathione Reductase - genetics</topic><topic>Glutathione Reductase - metabolism</topic><topic>Intracellular</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular structure</topic><topic>NADP - chemistry</topic><topic>NADP - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Conformation, beta-Strand</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Reactive nitrogen species</topic><topic>Reactive oxygen species</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Research Communications</topic><topic>Streptococcus infections</topic><topic>Streptococcus pneumoniae</topic><topic>Streptococcus pneumoniae - chemistry</topic><topic>Streptococcus pneumoniae - enzymology</topic><topic>Structural Homology, Protein</topic><topic>Substrate Specificity</topic><topic>X‐ray crystallography</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sikanyika, Mwilye</creatorcontrib><creatorcontrib>Aragão, David</creatorcontrib><creatorcontrib>McDevitt, Christopher A.</creatorcontrib><creatorcontrib>Maher, Megan J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sikanyika, Mwilye</au><au>Aragão, David</au><au>McDevitt, Christopher A.</au><au>Maher, Megan J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The structure and activity of the glutathione reductase from Streptococcus pneumoniae</atitle><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><date>2019-01</date><risdate>2019</risdate><volume>75</volume><issue>1</issue><spage>54</spage><epage>61</epage><pages>54-61</pages><issn>2053-230X</issn><eissn>2053-230X</eissn><abstract>The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β‐sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 ± 24.7 µM) in comparison to other characterized GR enzymes.
The three‐dimensional crystal structure of the glutathione reductase from Streptococcus pneumoniae is reported at 2.56 Å resolution.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>30605126</pmid><doi>10.1107/S2053230X18016527</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-1596-4841</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2053-230X |
| ispartof | Acta crystallographica. Section F, Structural biology communications, 2019-01, Vol.75 (1), p.54-61 |
| issn | 2053-230X 2053-230X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6317452 |
| source | MEDLINE; Access via Wiley Online Library; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Biocatalysis Cloning, Molecular Crystal structure Crystallography, X-Ray Cytoplasm Detoxification Dimers Enzymes Escherichia coli - genetics Escherichia coli - metabolism Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Glutathione Glutathione - chemistry Glutathione - metabolism Glutathione reductase Glutathione Reductase - chemistry Glutathione Reductase - genetics Glutathione Reductase - metabolism Intracellular Kinetics Models, Molecular Molecular structure NADP - chemistry NADP - metabolism Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Multimerization Reactive nitrogen species Reactive oxygen species Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Research Communications Streptococcus infections Streptococcus pneumoniae Streptococcus pneumoniae - chemistry Streptococcus pneumoniae - enzymology Structural Homology, Protein Substrate Specificity X‐ray crystallography Zinc |
| title | The structure and activity of the glutathione reductase from Streptococcus pneumoniae |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T16%3A36%3A09IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20structure%20and%20activity%20of%20the%20glutathione%20reductase%20from%20Streptococcus%20pneumoniae&rft.jtitle=Acta%20crystallographica.%20Section%20F,%20Structural%20biology%20communications&rft.au=Sikanyika,%20Mwilye&rft.date=2019-01&rft.volume=75&rft.issue=1&rft.spage=54&rft.epage=61&rft.pages=54-61&rft.issn=2053-230X&rft.eissn=2053-230X&rft_id=info:doi/10.1107/S2053230X18016527&rft_dat=%3Cproquest_pubme%3E2163012248%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2162784002&rft_id=info:pmid/30605126&rfr_iscdi=true |