Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum
The crystal structure of the F -catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F -ATPases from Caldalk...
Gespeichert in:
| Veröffentlicht in: | Open biology 2019-06, Vol.9 (6), p.190066 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 6 |
| container_start_page | 190066 |
| container_title | Open biology |
| container_volume | 9 |
| creator | Petri, Jessica Nakatani, Yoshio Montgomery, Martin G Ferguson, Scott A Aragão, David Leslie, Andrew G W Heikal, Adam Walker, John E Cook, Gregory M |
| description | The crystal structure of the F
-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F
-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β
-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria. |
| doi_str_mv | 10.1098/rsob.190066 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1098_rsob_190066</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>31238823</sourcerecordid><originalsourceid>FETCH-LOGICAL-c223t-fac7f0777bc9c8ac87c4d7029864c7ff094cbadef4f0a5b41870bd8ea5fbc43c3</originalsourceid><addsrcrecordid>eNpNkE1LAzEQhoMottSevEvusjVf3WSPpbhVLChYz8tkNtFKt1vycfDfu6UqzmWGdx5m4CHkmrMZZ5W5C7G3M14xVpZnZCyYKguhFD__N4_INMZPNtS85JXil2QkuZDGCDkmT68pZEw5ONp7WlNOi8XmBaKjPvQdTR9Dbnfbd0iOwh5c6K2jdR6-AiYXtrmj-4w7Byl3V-TCwy666U-fkLf6frN8KNbPq8flYl2gEDIVHlB7prW2WKEBNBpVq5moTKmGjWeVQgut88ozmFvFjWa2NQ7m3qKSKCfk9nQXQx9jcL45hG0H4avhrDlaaY5WmpOVgb450YdsO9f-sb8O5Dfj6V5E</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Royal Society Open Access Journals</source><source>PubMed Central Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Petri, Jessica ; Nakatani, Yoshio ; Montgomery, Martin G ; Ferguson, Scott A ; Aragão, David ; Leslie, Andrew G W ; Heikal, Adam ; Walker, John E ; Cook, Gregory M</creator><creatorcontrib>Petri, Jessica ; Nakatani, Yoshio ; Montgomery, Martin G ; Ferguson, Scott A ; Aragão, David ; Leslie, Andrew G W ; Heikal, Adam ; Walker, John E ; Cook, Gregory M</creatorcontrib><description>The crystal structure of the F
-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F
-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β
-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.</description><identifier>ISSN: 2046-2441</identifier><identifier>EISSN: 2046-2441</identifier><identifier>DOI: 10.1098/rsob.190066</identifier><identifier>PMID: 31238823</identifier><language>eng</language><publisher>England</publisher><subject>Adenosine Diphosphate - metabolism ; Bacterial Proteins - chemistry ; Crystallography, X-Ray ; Fusobacterium nucleatum - chemistry ; Fusobacterium nucleatum - enzymology ; Hydrolysis ; Models, Molecular ; Molecular Conformation ; Protein Domains ; Proton-Translocating ATPases - chemistry ; Proton-Translocating ATPases - metabolism</subject><ispartof>Open biology, 2019-06, Vol.9 (6), p.190066</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c223t-fac7f0777bc9c8ac87c4d7029864c7ff094cbadef4f0a5b41870bd8ea5fbc43c3</citedby><cites>FETCH-LOGICAL-c223t-fac7f0777bc9c8ac87c4d7029864c7ff094cbadef4f0a5b41870bd8ea5fbc43c3</cites><orcidid>0000-0001-8349-1500 ; 0000-0002-6551-4657</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,864,3313,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31238823$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Petri, Jessica</creatorcontrib><creatorcontrib>Nakatani, Yoshio</creatorcontrib><creatorcontrib>Montgomery, Martin G</creatorcontrib><creatorcontrib>Ferguson, Scott A</creatorcontrib><creatorcontrib>Aragão, David</creatorcontrib><creatorcontrib>Leslie, Andrew G W</creatorcontrib><creatorcontrib>Heikal, Adam</creatorcontrib><creatorcontrib>Walker, John E</creatorcontrib><creatorcontrib>Cook, Gregory M</creatorcontrib><title>Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum</title><title>Open biology</title><addtitle>Open Biol</addtitle><description>The crystal structure of the F
-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F
-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β
-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Crystallography, X-Ray</subject><subject>Fusobacterium nucleatum - chemistry</subject><subject>Fusobacterium nucleatum - enzymology</subject><subject>Hydrolysis</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Protein Domains</subject><subject>Proton-Translocating ATPases - chemistry</subject><subject>Proton-Translocating ATPases - metabolism</subject><issn>2046-2441</issn><issn>2046-2441</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkE1LAzEQhoMottSevEvusjVf3WSPpbhVLChYz8tkNtFKt1vycfDfu6UqzmWGdx5m4CHkmrMZZ5W5C7G3M14xVpZnZCyYKguhFD__N4_INMZPNtS85JXil2QkuZDGCDkmT68pZEw5ONp7WlNOi8XmBaKjPvQdTR9Dbnfbd0iOwh5c6K2jdR6-AiYXtrmj-4w7Byl3V-TCwy666U-fkLf6frN8KNbPq8flYl2gEDIVHlB7prW2WKEBNBpVq5moTKmGjWeVQgut88ozmFvFjWa2NQ7m3qKSKCfk9nQXQx9jcL45hG0H4avhrDlaaY5WmpOVgb450YdsO9f-sb8O5Dfj6V5E</recordid><startdate>20190601</startdate><enddate>20190601</enddate><creator>Petri, Jessica</creator><creator>Nakatani, Yoshio</creator><creator>Montgomery, Martin G</creator><creator>Ferguson, Scott A</creator><creator>Aragão, David</creator><creator>Leslie, Andrew G W</creator><creator>Heikal, Adam</creator><creator>Walker, John E</creator><creator>Cook, Gregory M</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0001-8349-1500</orcidid><orcidid>https://orcid.org/0000-0002-6551-4657</orcidid></search><sort><creationdate>20190601</creationdate><title>Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum</title><author>Petri, Jessica ; Nakatani, Yoshio ; Montgomery, Martin G ; Ferguson, Scott A ; Aragão, David ; Leslie, Andrew G W ; Heikal, Adam ; Walker, John E ; Cook, Gregory M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c223t-fac7f0777bc9c8ac87c4d7029864c7ff094cbadef4f0a5b41870bd8ea5fbc43c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Crystallography, X-Ray</topic><topic>Fusobacterium nucleatum - chemistry</topic><topic>Fusobacterium nucleatum - enzymology</topic><topic>Hydrolysis</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Protein Domains</topic><topic>Proton-Translocating ATPases - chemistry</topic><topic>Proton-Translocating ATPases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Petri, Jessica</creatorcontrib><creatorcontrib>Nakatani, Yoshio</creatorcontrib><creatorcontrib>Montgomery, Martin G</creatorcontrib><creatorcontrib>Ferguson, Scott A</creatorcontrib><creatorcontrib>Aragão, David</creatorcontrib><creatorcontrib>Leslie, Andrew G W</creatorcontrib><creatorcontrib>Heikal, Adam</creatorcontrib><creatorcontrib>Walker, John E</creatorcontrib><creatorcontrib>Cook, Gregory M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Open biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Petri, Jessica</au><au>Nakatani, Yoshio</au><au>Montgomery, Martin G</au><au>Ferguson, Scott A</au><au>Aragão, David</au><au>Leslie, Andrew G W</au><au>Heikal, Adam</au><au>Walker, John E</au><au>Cook, Gregory M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum</atitle><jtitle>Open biology</jtitle><addtitle>Open Biol</addtitle><date>2019-06-01</date><risdate>2019</risdate><volume>9</volume><issue>6</issue><spage>190066</spage><pages>190066-</pages><issn>2046-2441</issn><eissn>2046-2441</eissn><abstract>The crystal structure of the F
-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F
-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β
-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.</abstract><cop>England</cop><pmid>31238823</pmid><doi>10.1098/rsob.190066</doi><orcidid>https://orcid.org/0000-0001-8349-1500</orcidid><orcidid>https://orcid.org/0000-0002-6551-4657</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2046-2441 |
| ispartof | Open biology, 2019-06, Vol.9 (6), p.190066 |
| issn | 2046-2441 2046-2441 |
| language | eng |
| recordid | cdi_crossref_primary_10_1098_rsob_190066 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Royal Society Open Access Journals; PubMed Central Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adenosine Diphosphate - metabolism Bacterial Proteins - chemistry Crystallography, X-Ray Fusobacterium nucleatum - chemistry Fusobacterium nucleatum - enzymology Hydrolysis Models, Molecular Molecular Conformation Protein Domains Proton-Translocating ATPases - chemistry Proton-Translocating ATPases - metabolism |
| title | Structure of F 1 -ATPase from the obligate anaerobe Fusobacterium nucleatum |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T01%3A33%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20of%20F%201%20-ATPase%20from%20the%20obligate%20anaerobe%20Fusobacterium%20nucleatum&rft.jtitle=Open%20biology&rft.au=Petri,%20Jessica&rft.date=2019-06-01&rft.volume=9&rft.issue=6&rft.spage=190066&rft.pages=190066-&rft.issn=2046-2441&rft.eissn=2046-2441&rft_id=info:doi/10.1098/rsob.190066&rft_dat=%3Cpubmed_cross%3E31238823%3C/pubmed_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/31238823&rfr_iscdi=true |