Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes
Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane‐bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional me...
Gespeichert in:
| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-02, Vol.58 (2), p.341-342 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 342 |
|---|---|
| container_issue | 2 |
| container_start_page | 341 |
| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 58 |
| creator | Einsle, Oliver Stach, Petra Messerschmidt, Albrecht Klimmek, Oliver Simon, Jörg Kröger, Achim Kroneck, Peter M. H. |
| description | Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane‐bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane‐bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422. |
| doi_str_mv | 10.1107/S090744490102039X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71421224</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71421224</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3846-24c99d220507dcec55a5a384ed1f1e71e25e03fc2e19a575938f9c4b41ffca8d3</originalsourceid><addsrcrecordid>eNqFkcFu1DAQhiNERUvhAbggnxAcUsaOs46Pqy20VO2CRKHbk-V1xtTgxIudiKYvwSvjaleAxIHTjMbf98uaKYpnFI4oBfH6I0gQnHMJFBhUcvWgOKCVlCUAFw__6veLxyl9BQDGKvGo2Ke0AcEEPSh-LuKUBu29u9ODCz3RfUs2Eb3rXK_jRFZl1FOeaj8ll0iwZLhB0mG3jrrHch3GLJhpCOYmhg6JIb0bohuQRGxHM-iUZ6HbeLwlL5fRns5fEZtJchW869F7TdJojOvDF-wxPSn2rPYJn-7qYfHp7ZvLxWl5_v7k3WJ-Xpqq4bOScSNlyxjUIFqDpq51rfMLttRSFBRZjVBZw5BKXYtaVo2Vhq85tdbopq0Oixfb3E0M30dMg-pcMvff6TGMSQnKGWWMZ5BuQRNDShGt2kTX5c0oCur-CuqfK2Tn-S58XHfY_jF2a89AswV-OI_T_xPV_Pp4cQ1AZ1ktt6pLA97-VnX8pmaiErW6Wp6o5eeLs7PV5QfVVL8ARAmk_w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71421224</pqid></control><display><type>article</type><title>Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Alma/SFX Local Collection</source><creator>Einsle, Oliver ; Stach, Petra ; Messerschmidt, Albrecht ; Klimmek, Oliver ; Simon, Jörg ; Kröger, Achim ; Kroneck, Peter M. H.</creator><creatorcontrib>Einsle, Oliver ; Stach, Petra ; Messerschmidt, Albrecht ; Klimmek, Oliver ; Simon, Jörg ; Kröger, Achim ; Kroneck, Peter M. H.</creatorcontrib><description>Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane‐bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane‐bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S090744490102039X</identifier><identifier>PMID: 11807271</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Cell Membrane - metabolism ; Crystallization ; Crystallography, X-Ray ; cytochrome c nitrite reductase ; Cytochromes a1 ; Cytochromes c1 ; Models, Molecular ; Nitrate Reductases - chemistry ; Nitrate Reductases - metabolism ; Oxidoreductases - chemistry ; Oxidoreductases - metabolism ; Protein Conformation ; RNA-Binding Proteins ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Wolinella - enzymology</subject><ispartof>Acta crystallographica. Section D, Biological crystallography., 2002-02, Vol.58 (2), p.341-342</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3846-24c99d220507dcec55a5a384ed1f1e71e25e03fc2e19a575938f9c4b41ffca8d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1107%2FS090744490102039X$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1107%2FS090744490102039X$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11807271$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Einsle, Oliver</creatorcontrib><creatorcontrib>Stach, Petra</creatorcontrib><creatorcontrib>Messerschmidt, Albrecht</creatorcontrib><creatorcontrib>Klimmek, Oliver</creatorcontrib><creatorcontrib>Simon, Jörg</creatorcontrib><creatorcontrib>Kröger, Achim</creatorcontrib><creatorcontrib>Kroneck, Peter M. H.</creatorcontrib><title>Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane‐bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane‐bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>cytochrome c nitrite reductase</subject><subject>Cytochromes a1</subject><subject>Cytochromes c1</subject><subject>Models, Molecular</subject><subject>Nitrate Reductases - chemistry</subject><subject>Nitrate Reductases - metabolism</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - metabolism</subject><subject>Protein Conformation</subject><subject>RNA-Binding Proteins</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>Wolinella - enzymology</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhiNERUvhAbggnxAcUsaOs46Pqy20VO2CRKHbk-V1xtTgxIudiKYvwSvjaleAxIHTjMbf98uaKYpnFI4oBfH6I0gQnHMJFBhUcvWgOKCVlCUAFw__6veLxyl9BQDGKvGo2Ke0AcEEPSh-LuKUBu29u9ODCz3RfUs2Eb3rXK_jRFZl1FOeaj8ll0iwZLhB0mG3jrrHch3GLJhpCOYmhg6JIb0bohuQRGxHM-iUZ6HbeLwlL5fRns5fEZtJchW869F7TdJojOvDF-wxPSn2rPYJn-7qYfHp7ZvLxWl5_v7k3WJ-Xpqq4bOScSNlyxjUIFqDpq51rfMLttRSFBRZjVBZw5BKXYtaVo2Vhq85tdbopq0Oixfb3E0M30dMg-pcMvff6TGMSQnKGWWMZ5BuQRNDShGt2kTX5c0oCur-CuqfK2Tn-S58XHfY_jF2a89AswV-OI_T_xPV_Pp4cQ1AZ1ktt6pLA97-VnX8pmaiErW6Wp6o5eeLs7PV5QfVVL8ARAmk_w</recordid><startdate>200202</startdate><enddate>200202</enddate><creator>Einsle, Oliver</creator><creator>Stach, Petra</creator><creator>Messerschmidt, Albrecht</creator><creator>Klimmek, Oliver</creator><creator>Simon, Jörg</creator><creator>Kröger, Achim</creator><creator>Kroneck, Peter M. H.</creator><general>Munksgaard International Publishers</general><scope>BSCLL</scope><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>200202</creationdate><title>Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes</title><author>Einsle, Oliver ; Stach, Petra ; Messerschmidt, Albrecht ; Klimmek, Oliver ; Simon, Jörg ; Kröger, Achim ; Kroneck, Peter M. H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3846-24c99d220507dcec55a5a384ed1f1e71e25e03fc2e19a575938f9c4b41ffca8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>cytochrome c nitrite reductase</topic><topic>Cytochromes a1</topic><topic>Cytochromes c1</topic><topic>Models, Molecular</topic><topic>Nitrate Reductases - chemistry</topic><topic>Nitrate Reductases - metabolism</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - metabolism</topic><topic>Protein Conformation</topic><topic>RNA-Binding Proteins</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><topic>Wolinella - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Einsle, Oliver</creatorcontrib><creatorcontrib>Stach, Petra</creatorcontrib><creatorcontrib>Messerschmidt, Albrecht</creatorcontrib><creatorcontrib>Klimmek, Oliver</creatorcontrib><creatorcontrib>Simon, Jörg</creatorcontrib><creatorcontrib>Kröger, Achim</creatorcontrib><creatorcontrib>Kroneck, Peter M. H.</creatorcontrib><collection>Istex</collection><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>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Einsle, Oliver</au><au>Stach, Petra</au><au>Messerschmidt, Albrecht</au><au>Klimmek, Oliver</au><au>Simon, Jörg</au><au>Kröger, Achim</au><au>Kroneck, Peter M. H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2002-02</date><risdate>2002</risdate><volume>58</volume><issue>2</issue><spage>341</spage><epage>342</epage><pages>341-342</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane‐bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane‐bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>11807271</pmid><doi>10.1107/S090744490102039X</doi><tpages>2</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1399-0047 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2002-02, Vol.58 (2), p.341-342 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71421224 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cell Membrane - metabolism Crystallization Crystallography, X-Ray cytochrome c nitrite reductase Cytochromes a1 Cytochromes c1 Models, Molecular Nitrate Reductases - chemistry Nitrate Reductases - metabolism Oxidoreductases - chemistry Oxidoreductases - metabolism Protein Conformation RNA-Binding Proteins Transcription Factors - chemistry Transcription Factors - metabolism Wolinella - enzymology |
| title | Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T22%3A34%3A01IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallization%20and%20preliminary%20X-ray%20analysis%20of%20the%20membrane-bound%20cytochrome%20c%20nitrite%20reductase%20complex%20(NrfHA)%20from%20Wolinella%20succinogenes&rft.jtitle=Acta%20crystallographica.%20Section%20D,%20Biological%20crystallography.&rft.au=Einsle,%20Oliver&rft.date=2002-02&rft.volume=58&rft.issue=2&rft.spage=341&rft.epage=342&rft.pages=341-342&rft.issn=1399-0047&rft.eissn=1399-0047&rft_id=info:doi/10.1107/S090744490102039X&rft_dat=%3Cproquest_cross%3E71421224%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71421224&rft_id=info:pmid/11807271&rfr_iscdi=true |