1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein
Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing...
Gespeichert in:
| Veröffentlicht in: | Biomolecular NMR assignments 2023-12, Vol.17 (2), p.167-171 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 171 |
|---|---|
| container_issue | 2 |
| container_start_page | 167 |
| container_title | Biomolecular NMR assignments |
| container_volume | 17 |
| creator | Matosin, Srdan Fischer, Patrick D. Droemer, Maxim A. Baggs, Eric Chowdhury, Abu Sayeed Tavares, Isidoro Ficarro, Scott B. Warner, Lisa Rose Arthanari, Haribabu Nagarajan, Rajesh |
| description | Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing mechanisms. In this study, wehave expressed isotopically labeled holo-ACP from
Burkholderia mallei
in
Escherichia coli
to assign 100% of non-proline backbone amide (HN) resonances, 95.5% of aliphatic carbon resonances and 98.6% of aliphatic hydrogen sidechain resonances. |
| doi_str_mv | 10.1007/s12104-023-10136-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10676446</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2887038688</sourcerecordid><originalsourceid>FETCH-LOGICAL-c289t-9ded2cc265b283ae4bed622b91afce50cbd46be7d3a6fff2ee8852955e042ace3</originalsourceid><addsrcrecordid>eNp9kU9v1DAQxS1ERUvhC3CyxIUDoeM_cZwToiugSBVcQOJmOfZk121iL3aC1G9f062K4NDTjGZ-72lGj5BXDN4xgO6sMM5ANsBFw4AJ1cgn5ITpTja8g59PH3qmj8nzUq4AFAfOnpFj0XEhetmeEMsu3lImNtRGT1n7lQ7WXQ8p4t2gBI9uZ0OktpSwjTPGhaaRLjuk52u-3qXJYw6WznaaMFDrbibqbM4BM93ntGCIL8jRaKeCL-_rKfnx6eP3zUVz-e3zl82Hy8Zx3S9N79Fz57hqB66FRTmgV5wPPbOjwxbc4KUasPPCqnEcOaLWLe_bFkFy61CckvcH3_06zOhdPTXbyexzmG2-MckG8-8mhp3Zpt-GgeqUlKo6vLl3yOnXimUxcygOp8lGTGsxXHMAwXoBFX39H3qV1hzrf5XSHQittK4UP1Aup1Iyjg_XMDB_IjSHCE2N0NxFaGQViYOoVDhuMf-1fkR1C9LFnZ8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2887038688</pqid></control><display><type>article</type><title>1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein</title><source>SpringerLink Journals - AutoHoldings</source><creator>Matosin, Srdan ; Fischer, Patrick D. ; Droemer, Maxim A. ; Baggs, Eric ; Chowdhury, Abu Sayeed ; Tavares, Isidoro ; Ficarro, Scott B. ; Warner, Lisa Rose ; Arthanari, Haribabu ; Nagarajan, Rajesh</creator><creatorcontrib>Matosin, Srdan ; Fischer, Patrick D. ; Droemer, Maxim A. ; Baggs, Eric ; Chowdhury, Abu Sayeed ; Tavares, Isidoro ; Ficarro, Scott B. ; Warner, Lisa Rose ; Arthanari, Haribabu ; Nagarajan, Rajesh</creatorcontrib><description>Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing mechanisms. In this study, wehave expressed isotopically labeled holo-ACP from
Burkholderia mallei
in
Escherichia coli
to assign 100% of non-proline backbone amide (HN) resonances, 95.5% of aliphatic carbon resonances and 98.6% of aliphatic hydrogen sidechain resonances.</description><identifier>ISSN: 1874-2718</identifier><identifier>ISSN: 1874-270X</identifier><identifier>EISSN: 1874-270X</identifier><identifier>DOI: 10.1007/s12104-023-10136-4</identifier><identifier>PMID: 37233945</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Acyl carrier protein ; Biochemistry ; Biological and Medical Physics ; Biophysics ; Burkholderia mallei ; Endotoxins ; Lactones ; Physics ; Physics and Astronomy ; Polymer Sciences ; Quorum sensing</subject><ispartof>Biomolecular NMR assignments, 2023-12, Vol.17 (2), p.167-171</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Nature B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c289t-9ded2cc265b283ae4bed622b91afce50cbd46be7d3a6fff2ee8852955e042ace3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12104-023-10136-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12104-023-10136-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27923,27924,41487,42556,51318</link.rule.ids></links><search><creatorcontrib>Matosin, Srdan</creatorcontrib><creatorcontrib>Fischer, Patrick D.</creatorcontrib><creatorcontrib>Droemer, Maxim A.</creatorcontrib><creatorcontrib>Baggs, Eric</creatorcontrib><creatorcontrib>Chowdhury, Abu Sayeed</creatorcontrib><creatorcontrib>Tavares, Isidoro</creatorcontrib><creatorcontrib>Ficarro, Scott B.</creatorcontrib><creatorcontrib>Warner, Lisa Rose</creatorcontrib><creatorcontrib>Arthanari, Haribabu</creatorcontrib><creatorcontrib>Nagarajan, Rajesh</creatorcontrib><title>1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein</title><title>Biomolecular NMR assignments</title><addtitle>Biomol NMR Assign</addtitle><description>Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing mechanisms. In this study, wehave expressed isotopically labeled holo-ACP from
Burkholderia mallei
in
Escherichia coli
to assign 100% of non-proline backbone amide (HN) resonances, 95.5% of aliphatic carbon resonances and 98.6% of aliphatic hydrogen sidechain resonances.</description><subject>Acyl carrier protein</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Burkholderia mallei</subject><subject>Endotoxins</subject><subject>Lactones</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Polymer Sciences</subject><subject>Quorum sensing</subject><issn>1874-2718</issn><issn>1874-270X</issn><issn>1874-270X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kU9v1DAQxS1ERUvhC3CyxIUDoeM_cZwToiugSBVcQOJmOfZk121iL3aC1G9f062K4NDTjGZ-72lGj5BXDN4xgO6sMM5ANsBFw4AJ1cgn5ITpTja8g59PH3qmj8nzUq4AFAfOnpFj0XEhetmeEMsu3lImNtRGT1n7lQ7WXQ8p4t2gBI9uZ0OktpSwjTPGhaaRLjuk52u-3qXJYw6WznaaMFDrbibqbM4BM93ntGCIL8jRaKeCL-_rKfnx6eP3zUVz-e3zl82Hy8Zx3S9N79Fz57hqB66FRTmgV5wPPbOjwxbc4KUasPPCqnEcOaLWLe_bFkFy61CckvcH3_06zOhdPTXbyexzmG2-MckG8-8mhp3Zpt-GgeqUlKo6vLl3yOnXimUxcygOp8lGTGsxXHMAwXoBFX39H3qV1hzrf5XSHQittK4UP1Aup1Iyjg_XMDB_IjSHCE2N0NxFaGQViYOoVDhuMf-1fkR1C9LFnZ8</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Matosin, Srdan</creator><creator>Fischer, Patrick D.</creator><creator>Droemer, Maxim A.</creator><creator>Baggs, Eric</creator><creator>Chowdhury, Abu Sayeed</creator><creator>Tavares, Isidoro</creator><creator>Ficarro, Scott B.</creator><creator>Warner, Lisa Rose</creator><creator>Arthanari, Haribabu</creator><creator>Nagarajan, Rajesh</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20231201</creationdate><title>1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein</title><author>Matosin, Srdan ; Fischer, Patrick D. ; Droemer, Maxim A. ; Baggs, Eric ; Chowdhury, Abu Sayeed ; Tavares, Isidoro ; Ficarro, Scott B. ; Warner, Lisa Rose ; Arthanari, Haribabu ; Nagarajan, Rajesh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c289t-9ded2cc265b283ae4bed622b91afce50cbd46be7d3a6fff2ee8852955e042ace3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Acyl carrier protein</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Burkholderia mallei</topic><topic>Endotoxins</topic><topic>Lactones</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Polymer Sciences</topic><topic>Quorum sensing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matosin, Srdan</creatorcontrib><creatorcontrib>Fischer, Patrick D.</creatorcontrib><creatorcontrib>Droemer, Maxim A.</creatorcontrib><creatorcontrib>Baggs, Eric</creatorcontrib><creatorcontrib>Chowdhury, Abu Sayeed</creatorcontrib><creatorcontrib>Tavares, Isidoro</creatorcontrib><creatorcontrib>Ficarro, Scott B.</creatorcontrib><creatorcontrib>Warner, Lisa Rose</creatorcontrib><creatorcontrib>Arthanari, Haribabu</creatorcontrib><creatorcontrib>Nagarajan, Rajesh</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biomolecular NMR assignments</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matosin, Srdan</au><au>Fischer, Patrick D.</au><au>Droemer, Maxim A.</au><au>Baggs, Eric</au><au>Chowdhury, Abu Sayeed</au><au>Tavares, Isidoro</au><au>Ficarro, Scott B.</au><au>Warner, Lisa Rose</au><au>Arthanari, Haribabu</au><au>Nagarajan, Rajesh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein</atitle><jtitle>Biomolecular NMR assignments</jtitle><stitle>Biomol NMR Assign</stitle><date>2023-12-01</date><risdate>2023</risdate><volume>17</volume><issue>2</issue><spage>167</spage><epage>171</epage><pages>167-171</pages><issn>1874-2718</issn><issn>1874-270X</issn><eissn>1874-270X</eissn><abstract>Acyl carrier proteins (ACPs) are universally conserved proteins amongst different species and are involved in fatty acid synthesis. Bacteria utilize ACPs as acyl carriers and donors for the synthesis of products such as endotoxins or acyl homoserine lactones (AHLs), which are used in quorum sensing mechanisms. In this study, wehave expressed isotopically labeled holo-ACP from
Burkholderia mallei
in
Escherichia coli
to assign 100% of non-proline backbone amide (HN) resonances, 95.5% of aliphatic carbon resonances and 98.6% of aliphatic hydrogen sidechain resonances.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>37233945</pmid><doi>10.1007/s12104-023-10136-4</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1874-2718 |
| ispartof | Biomolecular NMR assignments, 2023-12, Vol.17 (2), p.167-171 |
| issn | 1874-2718 1874-270X 1874-270X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10676446 |
| source | SpringerLink Journals - AutoHoldings |
| subjects | Acyl carrier protein Biochemistry Biological and Medical Physics Biophysics Burkholderia mallei Endotoxins Lactones Physics Physics and Astronomy Polymer Sciences Quorum sensing |
| title | 1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T17%3A44%3A21IST&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=1H,%2013C%20and%2015N%20backbone%20and%20sidechain%20assignment%20of%20the%20Burkholderia%20mallei%20acyl%20carrier%20protein&rft.jtitle=Biomolecular%20NMR%20assignments&rft.au=Matosin,%20Srdan&rft.date=2023-12-01&rft.volume=17&rft.issue=2&rft.spage=167&rft.epage=171&rft.pages=167-171&rft.issn=1874-2718&rft.eissn=1874-270X&rft_id=info:doi/10.1007/s12104-023-10136-4&rft_dat=%3Cproquest_pubme%3E2887038688%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=2887038688&rft_id=info:pmid/37233945&rfr_iscdi=true |