A motif for quinone binding sites in respiratory and photosynthetic systems
Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centr...
Gespeichert in:
| Veröffentlicht in: | Journal of molecular biology 2000-03, Vol.296 (4), p.1153-1162 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1162 |
|---|---|
| container_issue | 4 |
| container_start_page | 1153 |
| container_title | Journal of molecular biology |
| container_volume | 296 |
| creator | Fisher, N Rich, P R |
| description | Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centres. We show here that a structural element containing a weak sequence motif is common to the Q(A) and Q(B) sites of bacterial reaction centres and the Q(i) site of the mitochondrial bc(1) complex. Analyses of sequence databases indicate that this element may also be present in the PsaA/B subunits of photosystem I, in the ND4 and ND5 subunits of complex I and, possibly, in the mitochondrial alternative quinol oxidase. This represents a first step in the structural classification of quinone binding sites. |
| doi_str_mv | 10.1006/jmbi.2000.3509 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_71022088</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71022088</sourcerecordid><originalsourceid>FETCH-LOGICAL-p207t-76dd3feb5eaf9d7bdcc3be8ad96fb450e624cd4cea8cb95e4aa3f7175216d63f3</originalsourceid><addsrcrecordid>eNo1jztPwzAYRT2AaCmsjMgTW4ofieOMVcVLVGKBOfLjM3XV2KntDPn3VAKmO9yjIx2E7ihZU0LE42HQfs0IIWvekO4CLQlhrGKSiwW6zvlwfhpeyyu0oERIQSldovcNHmLxDruY8GnyIQbA2gfrwzfOvkDGPuAEefRJlZhmrILF4z6WmOdQ9lC8wXnOBYZ8gy6dOma4_dsV-np--ty-VruPl7ftZleNjLSlaoW13IFuQLnOttoawzVIZTvhdN0QEKw2tjagpNFdA7VS3LW0bRgVVnDHV-jh1zumeJogl37w2cDxqALEKfctPXcTKc_g_R846QFsPyY_qDT3__n8BzdOXR8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71022088</pqid></control><display><type>article</type><title>A motif for quinone binding sites in respiratory and photosynthetic systems</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Fisher, N ; Rich, P R</creator><creatorcontrib>Fisher, N ; Rich, P R</creatorcontrib><description>Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centres. We show here that a structural element containing a weak sequence motif is common to the Q(A) and Q(B) sites of bacterial reaction centres and the Q(i) site of the mitochondrial bc(1) complex. Analyses of sequence databases indicate that this element may also be present in the PsaA/B subunits of photosystem I, in the ND4 and ND5 subunits of complex I and, possibly, in the mitochondrial alternative quinol oxidase. This represents a first step in the structural classification of quinone binding sites.</description><identifier>ISSN: 0022-2836</identifier><identifier>DOI: 10.1006/jmbi.2000.3509</identifier><identifier>PMID: 10686111</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Benzoquinones - metabolism ; Binding Sites ; Chlamydomonas - chemistry ; Chlorobi - chemistry ; Electron Transport Complex III - metabolism ; Molecular Sequence Data ; Photosynthetic Reaction Center Complex Proteins - chemistry ; Photosynthetic Reaction Center Complex Proteins - metabolism ; Photosystem I Protein Complex ; Protein Structure, Tertiary ; Rhodobacter - chemistry ; Sequence Homology, Amino Acid ; Space life sciences ; Vitamin K 1 - metabolism</subject><ispartof>Journal of molecular biology, 2000-03, Vol.296 (4), p.1153-1162</ispartof><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10686111$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fisher, N</creatorcontrib><creatorcontrib>Rich, P R</creatorcontrib><title>A motif for quinone binding sites in respiratory and photosynthetic systems</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centres. We show here that a structural element containing a weak sequence motif is common to the Q(A) and Q(B) sites of bacterial reaction centres and the Q(i) site of the mitochondrial bc(1) complex. Analyses of sequence databases indicate that this element may also be present in the PsaA/B subunits of photosystem I, in the ND4 and ND5 subunits of complex I and, possibly, in the mitochondrial alternative quinol oxidase. This represents a first step in the structural classification of quinone binding sites.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Benzoquinones - metabolism</subject><subject>Binding Sites</subject><subject>Chlamydomonas - chemistry</subject><subject>Chlorobi - chemistry</subject><subject>Electron Transport Complex III - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Photosynthetic Reaction Center Complex Proteins - chemistry</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>Photosystem I Protein Complex</subject><subject>Protein Structure, Tertiary</subject><subject>Rhodobacter - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>Space life sciences</subject><subject>Vitamin K 1 - metabolism</subject><issn>0022-2836</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1jztPwzAYRT2AaCmsjMgTW4ofieOMVcVLVGKBOfLjM3XV2KntDPn3VAKmO9yjIx2E7ihZU0LE42HQfs0IIWvekO4CLQlhrGKSiwW6zvlwfhpeyyu0oERIQSldovcNHmLxDruY8GnyIQbA2gfrwzfOvkDGPuAEefRJlZhmrILF4z6WmOdQ9lC8wXnOBYZ8gy6dOma4_dsV-np--ty-VruPl7ftZleNjLSlaoW13IFuQLnOttoawzVIZTvhdN0QEKw2tjagpNFdA7VS3LW0bRgVVnDHV-jh1zumeJogl37w2cDxqALEKfctPXcTKc_g_R846QFsPyY_qDT3__n8BzdOXR8</recordid><startdate>20000303</startdate><enddate>20000303</enddate><creator>Fisher, N</creator><creator>Rich, P R</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20000303</creationdate><title>A motif for quinone binding sites in respiratory and photosynthetic systems</title><author>Fisher, N ; Rich, P R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p207t-76dd3feb5eaf9d7bdcc3be8ad96fb450e624cd4cea8cb95e4aa3f7175216d63f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Benzoquinones - metabolism</topic><topic>Binding Sites</topic><topic>Chlamydomonas - chemistry</topic><topic>Chlorobi - chemistry</topic><topic>Electron Transport Complex III - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Photosynthetic Reaction Center Complex Proteins - chemistry</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>Photosystem I Protein Complex</topic><topic>Protein Structure, Tertiary</topic><topic>Rhodobacter - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>Space life sciences</topic><topic>Vitamin K 1 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fisher, N</creatorcontrib><creatorcontrib>Rich, P R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fisher, N</au><au>Rich, P R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A motif for quinone binding sites in respiratory and photosynthetic systems</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2000-03-03</date><risdate>2000</risdate><volume>296</volume><issue>4</issue><spage>1153</spage><epage>1162</epage><pages>1153-1162</pages><issn>0022-2836</issn><abstract>Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centres. We show here that a structural element containing a weak sequence motif is common to the Q(A) and Q(B) sites of bacterial reaction centres and the Q(i) site of the mitochondrial bc(1) complex. Analyses of sequence databases indicate that this element may also be present in the PsaA/B subunits of photosystem I, in the ND4 and ND5 subunits of complex I and, possibly, in the mitochondrial alternative quinol oxidase. This represents a first step in the structural classification of quinone binding sites.</abstract><cop>England</cop><pmid>10686111</pmid><doi>10.1006/jmbi.2000.3509</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 2000-03, Vol.296 (4), p.1153-1162 |
| issn | 0022-2836 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71022088 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Benzoquinones - metabolism Binding Sites Chlamydomonas - chemistry Chlorobi - chemistry Electron Transport Complex III - metabolism Molecular Sequence Data Photosynthetic Reaction Center Complex Proteins - chemistry Photosynthetic Reaction Center Complex Proteins - metabolism Photosystem I Protein Complex Protein Structure, Tertiary Rhodobacter - chemistry Sequence Homology, Amino Acid Space life sciences Vitamin K 1 - metabolism |
| title | A motif for quinone binding sites in respiratory and photosynthetic systems |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T13%3A51%3A59IST&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=A%20motif%20for%20quinone%20binding%20sites%20in%20respiratory%20and%20photosynthetic%20systems&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=Fisher,%20N&rft.date=2000-03-03&rft.volume=296&rft.issue=4&rft.spage=1153&rft.epage=1162&rft.pages=1153-1162&rft.issn=0022-2836&rft_id=info:doi/10.1006/jmbi.2000.3509&rft_dat=%3Cproquest_pubme%3E71022088%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=71022088&rft_id=info:pmid/10686111&rfr_iscdi=true |