Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase
The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Å resolution. Each monomer contains two α-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and s...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2002-11, Vol.99 (24), p.15375-15380 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 15380 |
|---|---|
| container_issue | 24 |
| container_start_page | 15375 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 99 |
| creator | Whittington, Douglas A. Wise, Mitchell L. Urbansky, Marek Coates, Robert M. Croteau, Rodney B. Christianson, David W. |
| description | The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Å resolution. Each monomer contains two α-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade. |
| doi_str_mv | 10.1073/pnas.232591099 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1073_pnas_232591099</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3073780</jstor_id><sourcerecordid>3073780</sourcerecordid><originalsourceid>FETCH-LOGICAL-c582t-6a34ec4627a6374f415a7341b18c62ed9d7e4a65060c3e17b7e0b1a79403f9f03</originalsourceid><addsrcrecordid>eNp9kUuv0zAQhS0E4pbClhUCwwKxafErcYzEAspTuojFvawtx3EaV6kdbAeRf49DSnkskBej0XwzPjMHgPsYbTHi9PngVNwSSgqBkRA3wCoHvCmZQDfBCiHCNxUj7ALcifGAEBJFhW6DC0wYJUiUK7B_7YObevjGDp2PQ6eSgVeTS52K5gW8SmHUaQwGKtfMWS7vJ9j6AHcq1F6rZL2Dn5Szw9gvST1BBa9NGIzztoG7Sfd51l1wq1V9NPdOcQ2-vHt7vfuwufz8_uPu1eVGFxVJm1JRZjQrCVcl5axluFCcMlzjSpfENKLhhqmyQCXS1GBec4NqrLhgiLaiRXQNXi5zh7E-mkYbl0X3cgj2qMIkvbLy74qzndz7bxJTzvNV1uDx0u9jsjJqm4zutHfO6CQrnM-MM_P09EfwX0cTkzzaqE3fK2f8GCUn-XFeZPDJP-DBj8Hl_SVBmIqZytB2gXTwMQbTnsViJGeP5eyxPHucGx7-ueJv_GRqBh6dgLnxV1kISZjEBf0p7Nn_CdmOfZ_M95TRBwt6iMmHM0uzMF4h-gPIscUC</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201392777</pqid></control><display><type>article</type><title>Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Whittington, Douglas A. ; Wise, Mitchell L. ; Urbansky, Marek ; Coates, Robert M. ; Croteau, Rodney B. ; Christianson, David W.</creator><creatorcontrib>Whittington, Douglas A. ; Wise, Mitchell L. ; Urbansky, Marek ; Coates, Robert M. ; Croteau, Rodney B. ; Christianson, David W. ; Stanford Synchrotron Radiation Lab. (US) ; Stanford Linear Accelerator Center, Menlo Park, CA (US)</creatorcontrib><description>The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Å resolution. Each monomer contains two α-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.232591099</identifier><identifier>PMID: 12432096</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Active sites ; Atoms ; BASIC BIOLOGICAL SCIENCES ; Binding Sites ; Biochemistry ; Biological Sciences ; Catalysis ; Crystals ; CYCLASES ; Diphosphates ; DNA, Complementary - genetics ; Enzymes ; Hydrogen bonds ; Intramolecular Lyases - chemistry ; Intramolecular Lyases - physiology ; Metals ; Models, Molecular ; Molecules ; Monomers ; Monoterpenes ; Monoterpenes - metabolism ; Plant Proteins - chemistry ; Plant Proteins - physiology ; Protein Conformation ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Recombinant Fusion Proteins - chemistry ; Salvia - enzymology ; Sesquiterpenes ; STANFORD LINEAR ACCELERATOR CENTER ; STANFORD SYNCHROTRON RADIATION LABORATORY ; Structure-Activity Relationship ; SYNCHROTRON RADIATION ; Terpenoids</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2002-11, Vol.99 (24), p.15375-15380</ispartof><rights>Copyright 1993-2002 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 26, 2002</rights><rights>Copyright © 2002, The National Academy of Sciences</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c582t-6a34ec4627a6374f415a7341b18c62ed9d7e4a65060c3e17b7e0b1a79403f9f03</citedby><cites>FETCH-LOGICAL-c582t-6a34ec4627a6374f415a7341b18c62ed9d7e4a65060c3e17b7e0b1a79403f9f03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/99/24.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3073780$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3073780$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12432096$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/815911$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Whittington, Douglas A.</creatorcontrib><creatorcontrib>Wise, Mitchell L.</creatorcontrib><creatorcontrib>Urbansky, Marek</creatorcontrib><creatorcontrib>Coates, Robert M.</creatorcontrib><creatorcontrib>Croteau, Rodney B.</creatorcontrib><creatorcontrib>Christianson, David W.</creatorcontrib><creatorcontrib>Stanford Synchrotron Radiation Lab. (US)</creatorcontrib><creatorcontrib>Stanford Linear Accelerator Center, Menlo Park, CA (US)</creatorcontrib><title>Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase</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 dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Å resolution. Each monomer contains two α-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.</description><subject>Active sites</subject><subject>Atoms</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Catalysis</subject><subject>Crystals</subject><subject>CYCLASES</subject><subject>Diphosphates</subject><subject>DNA, Complementary - genetics</subject><subject>Enzymes</subject><subject>Hydrogen bonds</subject><subject>Intramolecular Lyases - chemistry</subject><subject>Intramolecular Lyases - physiology</subject><subject>Metals</subject><subject>Models, Molecular</subject><subject>Molecules</subject><subject>Monomers</subject><subject>Monoterpenes</subject><subject>Monoterpenes - metabolism</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - physiology</subject><subject>Protein Conformation</subject><subject>Protein Interaction Mapping</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Salvia - enzymology</subject><subject>Sesquiterpenes</subject><subject>STANFORD LINEAR ACCELERATOR CENTER</subject><subject>STANFORD SYNCHROTRON RADIATION LABORATORY</subject><subject>Structure-Activity Relationship</subject><subject>SYNCHROTRON RADIATION</subject><subject>Terpenoids</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuv0zAQhS0E4pbClhUCwwKxafErcYzEAspTuojFvawtx3EaV6kdbAeRf49DSnkskBej0XwzPjMHgPsYbTHi9PngVNwSSgqBkRA3wCoHvCmZQDfBCiHCNxUj7ALcifGAEBJFhW6DC0wYJUiUK7B_7YObevjGDp2PQ6eSgVeTS52K5gW8SmHUaQwGKtfMWS7vJ9j6AHcq1F6rZL2Dn5Szw9gvST1BBa9NGIzztoG7Sfd51l1wq1V9NPdOcQ2-vHt7vfuwufz8_uPu1eVGFxVJm1JRZjQrCVcl5axluFCcMlzjSpfENKLhhqmyQCXS1GBec4NqrLhgiLaiRXQNXi5zh7E-mkYbl0X3cgj2qMIkvbLy74qzndz7bxJTzvNV1uDx0u9jsjJqm4zutHfO6CQrnM-MM_P09EfwX0cTkzzaqE3fK2f8GCUn-XFeZPDJP-DBj8Hl_SVBmIqZytB2gXTwMQbTnsViJGeP5eyxPHucGx7-ueJv_GRqBh6dgLnxV1kISZjEBf0p7Nn_CdmOfZ_M95TRBwt6iMmHM0uzMF4h-gPIscUC</recordid><startdate>20021126</startdate><enddate>20021126</enddate><creator>Whittington, Douglas A.</creator><creator>Wise, Mitchell L.</creator><creator>Urbansky, Marek</creator><creator>Coates, Robert M.</creator><creator>Croteau, Rodney B.</creator><creator>Christianson, David W.</creator><general>National Academy of Sciences</general><general>National Acad 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>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20021126</creationdate><title>Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase</title><author>Whittington, Douglas A. ; Wise, Mitchell L. ; Urbansky, Marek ; Coates, Robert M. ; Croteau, Rodney B. ; Christianson, David W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c582t-6a34ec4627a6374f415a7341b18c62ed9d7e4a65060c3e17b7e0b1a79403f9f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Active sites</topic><topic>Atoms</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Catalysis</topic><topic>Crystals</topic><topic>CYCLASES</topic><topic>Diphosphates</topic><topic>DNA, Complementary - genetics</topic><topic>Enzymes</topic><topic>Hydrogen bonds</topic><topic>Intramolecular Lyases - chemistry</topic><topic>Intramolecular Lyases - physiology</topic><topic>Metals</topic><topic>Models, Molecular</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Monoterpenes</topic><topic>Monoterpenes - metabolism</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - physiology</topic><topic>Protein Conformation</topic><topic>Protein Interaction Mapping</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Salvia - enzymology</topic><topic>Sesquiterpenes</topic><topic>STANFORD LINEAR ACCELERATOR CENTER</topic><topic>STANFORD SYNCHROTRON RADIATION LABORATORY</topic><topic>Structure-Activity Relationship</topic><topic>SYNCHROTRON RADIATION</topic><topic>Terpenoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Whittington, Douglas A.</creatorcontrib><creatorcontrib>Wise, Mitchell L.</creatorcontrib><creatorcontrib>Urbansky, Marek</creatorcontrib><creatorcontrib>Coates, Robert M.</creatorcontrib><creatorcontrib>Croteau, Rodney B.</creatorcontrib><creatorcontrib>Christianson, David W.</creatorcontrib><creatorcontrib>Stanford Synchrotron Radiation Lab. (US)</creatorcontrib><creatorcontrib>Stanford Linear Accelerator Center, Menlo Park, CA (US)</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>OSTI.GOV</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>Whittington, Douglas A.</au><au>Wise, Mitchell L.</au><au>Urbansky, Marek</au><au>Coates, Robert M.</au><au>Croteau, Rodney B.</au><au>Christianson, David W.</au><aucorp>Stanford Synchrotron Radiation Lab. (US)</aucorp><aucorp>Stanford Linear Accelerator Center, Menlo Park, CA (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2002-11-26</date><risdate>2002</risdate><volume>99</volume><issue>24</issue><spage>15375</spage><epage>15380</epage><pages>15375-15380</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-Å resolution. Each monomer contains two α-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>12432096</pmid><doi>10.1073/pnas.232591099</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, 2002-11, Vol.99 (24), p.15375-15380 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_crossref_primary_10_1073_pnas_232591099 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Active sites Atoms BASIC BIOLOGICAL SCIENCES Binding Sites Biochemistry Biological Sciences Catalysis Crystals CYCLASES Diphosphates DNA, Complementary - genetics Enzymes Hydrogen bonds Intramolecular Lyases - chemistry Intramolecular Lyases - physiology Metals Models, Molecular Molecules Monomers Monoterpenes Monoterpenes - metabolism Plant Proteins - chemistry Plant Proteins - physiology Protein Conformation Protein Interaction Mapping Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Salvia - enzymology Sesquiterpenes STANFORD LINEAR ACCELERATOR CENTER STANFORD SYNCHROTRON RADIATION LABORATORY Structure-Activity Relationship SYNCHROTRON RADIATION Terpenoids |
| title | Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T16%3A48%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bornyl%20Diphosphate%20Synthase:%20Structure%20and%20Strategy%20for%20Carbocation%20Manipulation%20by%20a%20Terpenoid%20Cyclase&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Whittington,%20Douglas%20A.&rft.aucorp=Stanford%20Synchrotron%20Radiation%20Lab.%20(US)&rft.date=2002-11-26&rft.volume=99&rft.issue=24&rft.spage=15375&rft.epage=15380&rft.pages=15375-15380&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.232591099&rft_dat=%3Cjstor_cross%3E3073780%3C/jstor_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201392777&rft_id=info:pmid/12432096&rft_jstor_id=3073780&rfr_iscdi=true |