Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade
The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Å resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ions near the mouth of the active site cleft. A compariso...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2001-11, Vol.98 (24), p.13543-13548 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 13548 |
|---|---|
| container_issue | 24 |
| container_start_page | 13543 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 98 |
| creator | Rynkiewicz, Michael J. Cane, David E. Christianson, David W. |
| description | The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Å resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis. |
| doi_str_mv | 10.1073/pnas.231313098 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_journals_201391181</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3057130</jstor_id><sourcerecordid>3057130</sourcerecordid><originalsourceid>FETCH-LOGICAL-c520t-cc9d856bd2d4bfe3bed4f8d92badee4662b189ad661fd7fdd4f501302904069e3</originalsourceid><addsrcrecordid>eNqF0ktv1DAQAOAIgei2cOWEIOKAuGTxI3FiiQtaUahUBFKXs-XYE-JVYm9tp2J75Y_jdJflcQDlkMjzzWg8mSx7gtESo5q-3loZloTi9CDe3MsWGHFcsJKj-9kCIVIXTUnKk-w0hA1CiFcNepidYMx4w0q6yL5fRT-pOHnIXZevvVG90wYs5Fc7G3sZIO-8G_PzKUhvpjEPW-ddnJ1xRkPIP3t3c_fxEVQvrQnRqPzCduDBqnTsbB57yNfgt3PZ1U4N5lZGk85XMiip4VH2oJNDgMeH91n25fzdevWhuPz0_mL19rJQFUGxUIrrpmKtJrpsO6At6LJrNCdtqgElY6TFDZeaMdzputMpWqE0FsJRiRgHepa92dfdTu0IWoGNXg5i680o_U44acSfEWt68dXdCJZGXaf0l4d0764nCFGMJigYBmnBTUHUhCJE6f8hbjCpGa0SfPEX3LjJ2zQDQVLnHCeZ0HKPlHcheOiODWMk5h0Q8w6I4w6khGe_X_MXP_z0BJ4fwJz4M8wbQUqBaXUnXv1biG4ahgjfYqJP93QTovNHS1FVp3boD2re00Y</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201391181</pqid></control><display><type>article</type><title>Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Rynkiewicz, Michael J. ; Cane, David E. ; Christianson, David W.</creator><creatorcontrib>Rynkiewicz, Michael J. ; Cane, David E. ; Christianson, David W.</creatorcontrib><description>The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Å resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.231313098</identifier><identifier>PMID: 11698643</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Active sites ; Amino Acid Sequence ; Atoms ; Biological Sciences ; Biosynthesis ; Carbon-Carbon Lyases - chemistry ; Carbon-Carbon Lyases - metabolism ; Coordinate systems ; Crystallography ; Crystallography, X-Ray ; Diphosphates ; Diphosphates - chemistry ; Diphosphates - metabolism ; Enzymes ; Fusarium - enzymology ; Fusarium sporotrichioides ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Monomers ; Polymers ; Protein Structure, Tertiary ; Sesquiterpenes ; Terpenes ; Terpenes - metabolism ; Terpenoids</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2001-11, Vol.98 (24), p.13543-13548</ispartof><rights>Copyright 1993-2001 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 20, 2001</rights><rights>Copyright © 2001, The National Academy of Sciences 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-cc9d856bd2d4bfe3bed4f8d92badee4662b189ad661fd7fdd4f501302904069e3</citedby><cites>FETCH-LOGICAL-c520t-cc9d856bd2d4bfe3bed4f8d92badee4662b189ad661fd7fdd4f501302904069e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/98/24.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3057130$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3057130$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11698643$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rynkiewicz, Michael J.</creatorcontrib><creatorcontrib>Cane, David E.</creatorcontrib><creatorcontrib>Christianson, David W.</creatorcontrib><title>Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Å resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis.</description><subject>Active sites</subject><subject>Amino Acid Sequence</subject><subject>Atoms</subject><subject>Biological Sciences</subject><subject>Biosynthesis</subject><subject>Carbon-Carbon Lyases - chemistry</subject><subject>Carbon-Carbon Lyases - metabolism</subject><subject>Coordinate systems</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Diphosphates</subject><subject>Diphosphates - chemistry</subject><subject>Diphosphates - metabolism</subject><subject>Enzymes</subject><subject>Fusarium - enzymology</subject><subject>Fusarium sporotrichioides</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Monomers</subject><subject>Polymers</subject><subject>Protein Structure, Tertiary</subject><subject>Sesquiterpenes</subject><subject>Terpenes</subject><subject>Terpenes - metabolism</subject><subject>Terpenoids</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0ktv1DAQAOAIgei2cOWEIOKAuGTxI3FiiQtaUahUBFKXs-XYE-JVYm9tp2J75Y_jdJflcQDlkMjzzWg8mSx7gtESo5q-3loZloTi9CDe3MsWGHFcsJKj-9kCIVIXTUnKk-w0hA1CiFcNepidYMx4w0q6yL5fRT-pOHnIXZevvVG90wYs5Fc7G3sZIO-8G_PzKUhvpjEPW-ddnJ1xRkPIP3t3c_fxEVQvrQnRqPzCduDBqnTsbB57yNfgt3PZ1U4N5lZGk85XMiip4VH2oJNDgMeH91n25fzdevWhuPz0_mL19rJQFUGxUIrrpmKtJrpsO6At6LJrNCdtqgElY6TFDZeaMdzputMpWqE0FsJRiRgHepa92dfdTu0IWoGNXg5i680o_U44acSfEWt68dXdCJZGXaf0l4d0764nCFGMJigYBmnBTUHUhCJE6f8hbjCpGa0SfPEX3LjJ2zQDQVLnHCeZ0HKPlHcheOiODWMk5h0Q8w6I4w6khGe_X_MXP_z0BJ4fwJz4M8wbQUqBaXUnXv1biG4ahgjfYqJP93QTovNHS1FVp3boD2re00Y</recordid><startdate>20011120</startdate><enddate>20011120</enddate><creator>Rynkiewicz, Michael J.</creator><creator>Cane, David E.</creator><creator>Christianson, David W.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20011120</creationdate><title>Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade</title><author>Rynkiewicz, Michael J. ; Cane, David E. ; Christianson, David W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-cc9d856bd2d4bfe3bed4f8d92badee4662b189ad661fd7fdd4f501302904069e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Active sites</topic><topic>Amino Acid Sequence</topic><topic>Atoms</topic><topic>Biological Sciences</topic><topic>Biosynthesis</topic><topic>Carbon-Carbon Lyases - chemistry</topic><topic>Carbon-Carbon Lyases - metabolism</topic><topic>Coordinate systems</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Diphosphates</topic><topic>Diphosphates - chemistry</topic><topic>Diphosphates - metabolism</topic><topic>Enzymes</topic><topic>Fusarium - enzymology</topic><topic>Fusarium sporotrichioides</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Monomers</topic><topic>Polymers</topic><topic>Protein Structure, Tertiary</topic><topic>Sesquiterpenes</topic><topic>Terpenes</topic><topic>Terpenes - metabolism</topic><topic>Terpenoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rynkiewicz, Michael J.</creatorcontrib><creatorcontrib>Cane, David E.</creatorcontrib><creatorcontrib>Christianson, David W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rynkiewicz, Michael J.</au><au>Cane, David E.</au><au>Christianson, David W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2001-11-20</date><risdate>2001</risdate><volume>98</volume><issue>24</issue><spage>13543</spage><epage>13548</epage><pages>13543-13548</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Å resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11698643</pmid><doi>10.1073/pnas.231313098</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2001-11, Vol.98 (24), p.13543-13548 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_journals_201391181 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Active sites Amino Acid Sequence Atoms Biological Sciences Biosynthesis Carbon-Carbon Lyases - chemistry Carbon-Carbon Lyases - metabolism Coordinate systems Crystallography Crystallography, X-Ray Diphosphates Diphosphates - chemistry Diphosphates - metabolism Enzymes Fusarium - enzymology Fusarium sporotrichioides Ligands Models, Molecular Molecular Sequence Data Monomers Polymers Protein Structure, Tertiary Sesquiterpenes Terpenes Terpenes - metabolism Terpenoids |
| title | Structure of Trichodiene Synthase from Fusarium sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade |
| 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%3A51%3A39IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20of%20Trichodiene%20Synthase%20from%20Fusarium%20sporotrichioides%20Provides%20Mechanistic%20Inferences%20on%20the%20Terpene%20Cyclization%20Cascade&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Rynkiewicz,%20Michael%20J.&rft.date=2001-11-20&rft.volume=98&rft.issue=24&rft.spage=13543&rft.epage=13548&rft.pages=13543-13548&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.231313098&rft_dat=%3Cjstor_proqu%3E3057130%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201391181&rft_id=info:pmid/11698643&rft_jstor_id=3057130&rfr_iscdi=true |