Crystal structure of the Clostridium limosum C3 exoenzyme
C3-like toxins ADP-ribosylate and inactivate Rho GTPases. Seven C3-like ADP-ribosyltransferases produced by Clostridium botulinum, Clostridium limosum, Bacillus cereus and Staphylococcus aureus were identified and two representatives – C3bot from C. botulinum and C3stau2 from S. aureus – were crysta...
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| Veröffentlicht in: | FEBS letters 2008-04, Vol.582 (7), p.1032-1036 |
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| creator | Vogelsgesang, Martin Stieglitz, Benjamin Herrmann, Christian Pautsch, Alex Aktories, Klaus |
| description | C3-like toxins ADP-ribosylate and inactivate Rho GTPases. Seven C3-like ADP-ribosyltransferases produced by
Clostridium botulinum,
Clostridium limosum,
Bacillus cereus and
Staphylococcus aureus were identified and two representatives – C3bot from
C. botulinum and C3stau2 from
S. aureus – were crystallized. Here we present the 1.8
Å structure of
C. limosum C3 transferase C3lim and compare it to the structures of other family members. In contrast to the structure of apo-C3bot, the canonical ADP-ribosylating turn turn motif is observed in a primed conformation, ready for NAD binding. This suggests an impact on the binding mode of NAD and on the transferase reaction. The crystal structure explains why auto-ADP-ribosylation of C3lim at Arg41 interferes with the ADP-ribosyltransferase activity of the toxin. |
| doi_str_mv | 10.1016/j.febslet.2008.02.051 |
| format | Article |
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Clostridium botulinum,
Clostridium limosum,
Bacillus cereus and
Staphylococcus aureus were identified and two representatives – C3bot from
C. botulinum and C3stau2 from
S. aureus – were crystallized. Here we present the 1.8
Å structure of
C. limosum C3 transferase C3lim and compare it to the structures of other family members. In contrast to the structure of apo-C3bot, the canonical ADP-ribosylating turn turn motif is observed in a primed conformation, ready for NAD binding. This suggests an impact on the binding mode of NAD and on the transferase reaction. The crystal structure explains why auto-ADP-ribosylation of C3lim at Arg41 interferes with the ADP-ribosyltransferase activity of the toxin.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2008.02.051</identifier><identifier>PMID: 18325337</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>ADP Ribose Transferases - chemistry ; ADP-ribosylation toxin turn turn motif ; ADP-ribosyltransferase ; Amino Acid Sequence ; ARTT-motif ; Bacillus cereus ; Botulinum Toxins - chemistry ; C3 ADP-ribosyltransferase from Bacillus cereus ; C3 ADP-ribosyltransferase from Clostridium botulinum ; C3 ADP-ribosyltransferase from Clostridium limosum ; C3 ADP-ribosyltransferase from Staphylococcus aureus ; C3bot ; C3cer ; C3lim ; C3stau2 ; Clostridium ; Clostridium botulinum ; Crystal structure ; Crystallography, X-Ray ; Exoenzyme C3 ; glutathione S-transferase ; GST ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Rho GTPase ; Staphylococcus aureus ; Toxin</subject><ispartof>FEBS letters, 2008-04, Vol.582 (7), p.1032-1036</ispartof><rights>2008 Federation of European Biochemical Societies</rights><rights>FEBS Letters 582 (2008) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c572X-c764dba439eaadc6c19a8613317d95c634e750f66f1df31145dee2774b8d3fd73</citedby><cites>FETCH-LOGICAL-c572X-c764dba439eaadc6c19a8613317d95c634e750f66f1df31145dee2774b8d3fd73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2008.02.051$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2008.02.051$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18325337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vogelsgesang, Martin</creatorcontrib><creatorcontrib>Stieglitz, Benjamin</creatorcontrib><creatorcontrib>Herrmann, Christian</creatorcontrib><creatorcontrib>Pautsch, Alex</creatorcontrib><creatorcontrib>Aktories, Klaus</creatorcontrib><title>Crystal structure of the Clostridium limosum C3 exoenzyme</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>C3-like toxins ADP-ribosylate and inactivate Rho GTPases. Seven C3-like ADP-ribosyltransferases produced by
Clostridium botulinum,
Clostridium limosum,
Bacillus cereus and
Staphylococcus aureus were identified and two representatives – C3bot from
C. botulinum and C3stau2 from
S. aureus – were crystallized. Here we present the 1.8
Å structure of
C. limosum C3 transferase C3lim and compare it to the structures of other family members. In contrast to the structure of apo-C3bot, the canonical ADP-ribosylating turn turn motif is observed in a primed conformation, ready for NAD binding. This suggests an impact on the binding mode of NAD and on the transferase reaction. The crystal structure explains why auto-ADP-ribosylation of C3lim at Arg41 interferes with the ADP-ribosyltransferase activity of the toxin.</description><subject>ADP Ribose Transferases - chemistry</subject><subject>ADP-ribosylation toxin turn turn motif</subject><subject>ADP-ribosyltransferase</subject><subject>Amino Acid Sequence</subject><subject>ARTT-motif</subject><subject>Bacillus cereus</subject><subject>Botulinum Toxins - chemistry</subject><subject>C3 ADP-ribosyltransferase from Bacillus cereus</subject><subject>C3 ADP-ribosyltransferase from Clostridium botulinum</subject><subject>C3 ADP-ribosyltransferase from Clostridium limosum</subject><subject>C3 ADP-ribosyltransferase from Staphylococcus aureus</subject><subject>C3bot</subject><subject>C3cer</subject><subject>C3lim</subject><subject>C3stau2</subject><subject>Clostridium</subject><subject>Clostridium botulinum</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Exoenzyme C3</subject><subject>glutathione S-transferase</subject><subject>GST</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Rho GTPase</subject><subject>Staphylococcus aureus</subject><subject>Toxin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1Lw0AQhhdRbK3-BCUnb4m72exHTqKhtULBgwq9LenuBLckTd1N1Prr3dCCRz3NB--8MzyD0CXBCcGE36yTCla-hi5JMZYJThPMyBEaEyloTDMuj9EYY5LFTOR0hM68X-NQS5KfohGRNGWUijHKC7fzXVlHvnO97noHUVtF3RtERd2GnjW2b6LaNq0PsaARfLWw-d41cI5OqrL2cHGIE_Q6m74U83jx9PBY3C1izUS6jLXgmVmVGc2hLI3mmuSl5IRSIkzONKcZCIYrzitiKkpIxgxAKkS2koZWRtAJut77bl373oPvVGO9hrouN9D2XqWYc8GkDEK2F2rXeu-gUltnm9LtFMFqYKbW6sBMDcwUTlVgFuauDgv6VQPmd-oAKQjme8GnrWH3P1c1m96nz8MDBv5YhozzZbC63VtBIPZhwSmvLWw0GOtAd8q09o9rfwDhJZVV</recordid><startdate>20080402</startdate><enddate>20080402</enddate><creator>Vogelsgesang, Martin</creator><creator>Stieglitz, Benjamin</creator><creator>Herrmann, Christian</creator><creator>Pautsch, Alex</creator><creator>Aktories, Klaus</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope></search><sort><creationdate>20080402</creationdate><title>Crystal structure of the Clostridium limosum C3 exoenzyme</title><author>Vogelsgesang, Martin ; Stieglitz, Benjamin ; Herrmann, Christian ; Pautsch, Alex ; Aktories, Klaus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c572X-c764dba439eaadc6c19a8613317d95c634e750f66f1df31145dee2774b8d3fd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>ADP Ribose Transferases - chemistry</topic><topic>ADP-ribosylation toxin turn turn motif</topic><topic>ADP-ribosyltransferase</topic><topic>Amino Acid Sequence</topic><topic>ARTT-motif</topic><topic>Bacillus cereus</topic><topic>Botulinum Toxins - chemistry</topic><topic>C3 ADP-ribosyltransferase from Bacillus cereus</topic><topic>C3 ADP-ribosyltransferase from Clostridium botulinum</topic><topic>C3 ADP-ribosyltransferase from Clostridium limosum</topic><topic>C3 ADP-ribosyltransferase from Staphylococcus aureus</topic><topic>C3bot</topic><topic>C3cer</topic><topic>C3lim</topic><topic>C3stau2</topic><topic>Clostridium</topic><topic>Clostridium botulinum</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Exoenzyme C3</topic><topic>glutathione S-transferase</topic><topic>GST</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Rho GTPase</topic><topic>Staphylococcus aureus</topic><topic>Toxin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vogelsgesang, Martin</creatorcontrib><creatorcontrib>Stieglitz, Benjamin</creatorcontrib><creatorcontrib>Herrmann, Christian</creatorcontrib><creatorcontrib>Pautsch, Alex</creatorcontrib><creatorcontrib>Aktories, Klaus</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vogelsgesang, Martin</au><au>Stieglitz, Benjamin</au><au>Herrmann, Christian</au><au>Pautsch, Alex</au><au>Aktories, Klaus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the Clostridium limosum C3 exoenzyme</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2008-04-02</date><risdate>2008</risdate><volume>582</volume><issue>7</issue><spage>1032</spage><epage>1036</epage><pages>1032-1036</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>C3-like toxins ADP-ribosylate and inactivate Rho GTPases. Seven C3-like ADP-ribosyltransferases produced by
Clostridium botulinum,
Clostridium limosum,
Bacillus cereus and
Staphylococcus aureus were identified and two representatives – C3bot from
C. botulinum and C3stau2 from
S. aureus – were crystallized. Here we present the 1.8
Å structure of
C. limosum C3 transferase C3lim and compare it to the structures of other family members. In contrast to the structure of apo-C3bot, the canonical ADP-ribosylating turn turn motif is observed in a primed conformation, ready for NAD binding. This suggests an impact on the binding mode of NAD and on the transferase reaction. The crystal structure explains why auto-ADP-ribosylation of C3lim at Arg41 interferes with the ADP-ribosyltransferase activity of the toxin.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>18325337</pmid><doi>10.1016/j.febslet.2008.02.051</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | ADP Ribose Transferases - chemistry ADP-ribosylation toxin turn turn motif ADP-ribosyltransferase Amino Acid Sequence ARTT-motif Bacillus cereus Botulinum Toxins - chemistry C3 ADP-ribosyltransferase from Bacillus cereus C3 ADP-ribosyltransferase from Clostridium botulinum C3 ADP-ribosyltransferase from Clostridium limosum C3 ADP-ribosyltransferase from Staphylococcus aureus C3bot C3cer C3lim C3stau2 Clostridium Clostridium botulinum Crystal structure Crystallography, X-Ray Exoenzyme C3 glutathione S-transferase GST Models, Molecular Molecular Sequence Data Protein Conformation Rho GTPase Staphylococcus aureus Toxin |
| title | Crystal structure of the Clostridium limosum C3 exoenzyme |
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