Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products
Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrate...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2019-03, Vol.9 (1), p.4392-4392, Article 4392 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4392 |
|---|---|
| container_issue | 1 |
| container_start_page | 4392 |
| container_title | Scientific reports |
| container_volume | 9 |
| creator | Sullivan, Amy H. Dranow, David M. Horanyi, Peter S. Lorimer, Donald D. Edwards, Thomas E. Abendroth, Jan |
| description | Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen
A. baumanii
in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site. |
| doi_str_mv | 10.1038/s41598-019-40558-x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6416309</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2190995663</sourcerecordid><originalsourceid>FETCH-LOGICAL-c501t-e2fe912a6b69c33337d60f51a54e8407b9f96e2aa80ee88b12f819467d88c11a3</originalsourceid><addsrcrecordid>eNp9ks1u1TAQhSMEolXpC7BAFmzYBGzH8bU3SNUVf1IlNrC2HGfSuCR28Dhw-_b4klIKC2ZjS_PNmRn7VNVTRl8x2qjXKFirVU2ZrgVtW1UfHlSnnIq25g3nD-_dT6pzxGtaouVaMP24Ommokjsh6Wl12KcbzHYimNPq8poASRxIHr2dfQAyxxCXMeIy2gzkqw8WgQwpzuTClXyOnXUZEunsOtsQvCc-EBfnZYID-eHzSHDtinapRmJDT5YU-9IIn1SPBjshnN-eZ9WXd28_7z_Ul5_ef9xfXNaupSzXwAfQjFvZSe2aErte0qFlthWgBN11etASuLWKAijVMT4opoXc9Uo5xmxzVr3ZdJe1m6F3EMowk1mSn226MdF683cm-NFcxe9GCiYbqovA800gYvYGnc_gRhdDAJcNa4VQuyP08rZLit9WwGxmjw6myQaIKxrONGsk5UoV9MU_6HVcUyhvcKSo1q2UTaH4RrkUERMMdxMzao4GMJsBTDGA-WUAcyhFz-7velfy-7sL0GwAllS4gvSn939kfwK6lL7r</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2190995663</pqid></control><display><type>article</type><title>Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products</title><source>MEDLINE</source><source>Nature Free</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><source>Springer Nature OA Free Journals</source><creator>Sullivan, Amy H. ; Dranow, David M. ; Horanyi, Peter S. ; Lorimer, Donald D. ; Edwards, Thomas E. ; Abendroth, Jan</creator><creatorcontrib>Sullivan, Amy H. ; Dranow, David M. ; Horanyi, Peter S. ; Lorimer, Donald D. ; Edwards, Thomas E. ; Abendroth, Jan ; Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen
A. baumanii
in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-019-40558-x</identifier><identifier>PMID: 30867460</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/535/1266 ; 631/535/1266 ; Acinetobacter baumannii - enzymology ; Acinetobacter baumannii - metabolism ; Adenosine ; Adenosine diphosphate ; Adenosine Diphosphate - metabolism ; Adenosine triphosphate ; Adenosine Triphosphate - metabolism ; ATP ; BASIC BIOLOGICAL SCIENCES ; Catalytic Domain ; Crystallization ; Humanities and Social Sciences ; multidisciplinary ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor) - metabolism ; Science ; Science (multidisciplinary) ; Thiamine ; Thiamine Pyrophosphate - metabolism ; Vitamin B ; X-ray crystallography</subject><ispartof>Scientific reports, 2019-03, Vol.9 (1), p.4392-4392, Article 4392</ispartof><rights>The Author(s) 2019</rights><rights>This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c501t-e2fe912a6b69c33337d60f51a54e8407b9f96e2aa80ee88b12f819467d88c11a3</citedby><cites>FETCH-LOGICAL-c501t-e2fe912a6b69c33337d60f51a54e8407b9f96e2aa80ee88b12f819467d88c11a3</cites><orcidid>0000-0002-8229-3243 ; 0000000282293243</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6416309/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6416309/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30867460$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/servlets/purl/1544879$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Sullivan, Amy H.</creatorcontrib><creatorcontrib>Dranow, David M.</creatorcontrib><creatorcontrib>Horanyi, Peter S.</creatorcontrib><creatorcontrib>Lorimer, Donald D.</creatorcontrib><creatorcontrib>Edwards, Thomas E.</creatorcontrib><creatorcontrib>Abendroth, Jan</creatorcontrib><creatorcontrib>Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen
A. baumanii
in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.</description><subject>631/45/535/1266</subject><subject>631/535/1266</subject><subject>Acinetobacter baumannii - enzymology</subject><subject>Acinetobacter baumannii - metabolism</subject><subject>Adenosine</subject><subject>Adenosine diphosphate</subject><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine triphosphate</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>ATP</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Catalytic Domain</subject><subject>Crystallization</subject><subject>Humanities and Social Sciences</subject><subject>multidisciplinary</subject><subject>Phosphorylation</subject><subject>Phosphotransferases (Phosphate Group Acceptor) - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Thiamine</subject><subject>Thiamine Pyrophosphate - metabolism</subject><subject>Vitamin B</subject><subject>X-ray crystallography</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9ks1u1TAQhSMEolXpC7BAFmzYBGzH8bU3SNUVf1IlNrC2HGfSuCR28Dhw-_b4klIKC2ZjS_PNmRn7VNVTRl8x2qjXKFirVU2ZrgVtW1UfHlSnnIq25g3nD-_dT6pzxGtaouVaMP24Ommokjsh6Wl12KcbzHYimNPq8poASRxIHr2dfQAyxxCXMeIy2gzkqw8WgQwpzuTClXyOnXUZEunsOtsQvCc-EBfnZYID-eHzSHDtinapRmJDT5YU-9IIn1SPBjshnN-eZ9WXd28_7z_Ul5_ef9xfXNaupSzXwAfQjFvZSe2aErte0qFlthWgBN11etASuLWKAijVMT4opoXc9Uo5xmxzVr3ZdJe1m6F3EMowk1mSn226MdF683cm-NFcxe9GCiYbqovA800gYvYGnc_gRhdDAJcNa4VQuyP08rZLit9WwGxmjw6myQaIKxrONGsk5UoV9MU_6HVcUyhvcKSo1q2UTaH4RrkUERMMdxMzao4GMJsBTDGA-WUAcyhFz-7velfy-7sL0GwAllS4gvSn939kfwK6lL7r</recordid><startdate>20190313</startdate><enddate>20190313</enddate><creator>Sullivan, Amy H.</creator><creator>Dranow, David M.</creator><creator>Horanyi, Peter S.</creator><creator>Lorimer, Donald D.</creator><creator>Edwards, Thomas E.</creator><creator>Abendroth, Jan</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>OIOZB</scope><scope>OTOTI</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8229-3243</orcidid><orcidid>https://orcid.org/0000000282293243</orcidid></search><sort><creationdate>20190313</creationdate><title>Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products</title><author>Sullivan, Amy H. ; Dranow, David M. ; Horanyi, Peter S. ; Lorimer, Donald D. ; Edwards, Thomas E. ; Abendroth, Jan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c501t-e2fe912a6b69c33337d60f51a54e8407b9f96e2aa80ee88b12f819467d88c11a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>631/45/535/1266</topic><topic>631/535/1266</topic><topic>Acinetobacter baumannii - enzymology</topic><topic>Acinetobacter baumannii - metabolism</topic><topic>Adenosine</topic><topic>Adenosine diphosphate</topic><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine triphosphate</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>ATP</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Catalytic Domain</topic><topic>Crystallization</topic><topic>Humanities and Social Sciences</topic><topic>multidisciplinary</topic><topic>Phosphorylation</topic><topic>Phosphotransferases (Phosphate Group Acceptor) - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Thiamine</topic><topic>Thiamine Pyrophosphate - metabolism</topic><topic>Vitamin B</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sullivan, Amy H.</creatorcontrib><creatorcontrib>Dranow, David M.</creatorcontrib><creatorcontrib>Horanyi, Peter S.</creatorcontrib><creatorcontrib>Lorimer, Donald D.</creatorcontrib><creatorcontrib>Edwards, Thomas E.</creatorcontrib><creatorcontrib>Abendroth, Jan</creatorcontrib><creatorcontrib>Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV - Hybrid</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sullivan, Amy H.</au><au>Dranow, David M.</au><au>Horanyi, Peter S.</au><au>Lorimer, Donald D.</au><au>Edwards, Thomas E.</au><au>Abendroth, Jan</au><aucorp>Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-03-13</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>4392</spage><epage>4392</epage><pages>4392-4392</pages><artnum>4392</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen
A. baumanii
in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30867460</pmid><doi>10.1038/s41598-019-40558-x</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-8229-3243</orcidid><orcidid>https://orcid.org/0000000282293243</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2019-03, Vol.9 (1), p.4392-4392, Article 4392 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6416309 |
| source | MEDLINE; Nature Free; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 631/45/535/1266 631/535/1266 Acinetobacter baumannii - enzymology Acinetobacter baumannii - metabolism Adenosine Adenosine diphosphate Adenosine Diphosphate - metabolism Adenosine triphosphate Adenosine Triphosphate - metabolism ATP BASIC BIOLOGICAL SCIENCES Catalytic Domain Crystallization Humanities and Social Sciences multidisciplinary Phosphorylation Phosphotransferases (Phosphate Group Acceptor) - metabolism Science Science (multidisciplinary) Thiamine Thiamine Pyrophosphate - metabolism Vitamin B X-ray crystallography |
| title | Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-16T01%3A31%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=Crystal%20structures%20of%20thiamine%20monophosphate%20kinase%20from%20Acinetobacter%20baumannii%20in%20complex%20with%20substrates%20and%20products&rft.jtitle=Scientific%20reports&rft.au=Sullivan,%20Amy%20H.&rft.aucorp=Argonne%20National%20Laboratory%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2019-03-13&rft.volume=9&rft.issue=1&rft.spage=4392&rft.epage=4392&rft.pages=4392-4392&rft.artnum=4392&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/s41598-019-40558-x&rft_dat=%3Cproquest_pubme%3E2190995663%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=2190995663&rft_id=info:pmid/30867460&rfr_iscdi=true |