crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins
Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA₁₋₁₀₇) of the translocation domain...
Gespeichert in:
| Veröffentlicht in: | Molecular microbiology 2010-02, Vol.75 (3), p.623-636 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 636 |
|---|---|
| container_issue | 3 |
| container_start_page | 623 |
| container_title | Molecular microbiology |
| container_volume | 75 |
| creator | Zhang, Ying Li, Chan Vankemmelbeke, Mireille N Bardelang, Philip Paoli, Max Penfold, Christopher N James, Richard |
| description | Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA₁₋₁₀₇) of the translocation domain of colicin A (ColA) and TolB identified the TolB box as a 12-residue peptide that folded into a distorted hairpin within a central canyon of the β-propeller domain of TolB. Comparison of this structure with that of the colicin E9 (ColE9) TolB box-TolB complex, together with site-directed mutagenesis of the ColA TolB box residues, revealed important differences in the interaction of the two TolB boxes with an overlapping binding site on TolB. Substitution of the TolB box residues of ColA with those of ColE9 conferred the ability to competitively recruit TolB from Pal but reduced the biological activity of the mutant ColA. This datum explains (i) the difference in binding affinities of ColA and ColE9 with TolB, and (ii) the inability of ColA, unlike ColE9, to competitively recruit TolB from Pal, allowing an understanding of how these two colicins interact in a different way with a common translocation portal in E. coli cells. |
| doi_str_mv | 10.1111/j.1365-2958.2009.06808.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2821528</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1948283651</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5228-b1535593066c8403f16b479e366bf19a88ea5eb1c73161876dc459aedb9db2573</originalsourceid><addsrcrecordid>eNqNUstu1DAUtRCIDoVfAAuJZYIf48RegNRWFCq1YkErsbMcx5nxKImD7bQzH8b_1WmiAXZk4cS55-WcAAAxynG6Pu5yTAuWEcF4ThASOSo44vn-GVgdB8_BCgmGMsrJzxPwKoQdQpiigr4EJ1gUpGSIrMBv7Q8hqhaG6EcdR2-ga2DcGnjr2nNYuf2016612vbwDKZFu25ozR4-2LidUd7cG9UGaLvB-aj6CGvbNMabXpswUSY9b7QfbexMGi8WSalz_awRvepD67SKNr160mnhGEwNqwPceDcOyX3JEV6DF00yNG-W-ym4u_xye_Etu_7-9eri7DrTjBCeVZhRxkQ6dKH5GtEGF9W6FIYWRdVgoTg3ipkK65LiAvOyqPWaCWXqStQVYSU9BZ9n3WGsOlPrlN2rVg7edsofpFNW_jvp7VZu3L0knGBGeBJ4vwh492s0IcqdG32fMsvUAcMIi3UC8RmkvQvBm-ZogJGc-pY7OdUqp1rl1Ld86lvuE_Xt3wH_EJeCE-DDAlBBq7ZJX1nbcMQRQjHndDrppxn3YFtz-O8A8ubmanpK_Hczv1FOqo1PHnc_yPTD4ZJwzjF9BF0-05k</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>196510194</pqid></control><display><type>article</type><title>crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Zhang, Ying ; Li, Chan ; Vankemmelbeke, Mireille N ; Bardelang, Philip ; Paoli, Max ; Penfold, Christopher N ; James, Richard</creator><creatorcontrib>Zhang, Ying ; Li, Chan ; Vankemmelbeke, Mireille N ; Bardelang, Philip ; Paoli, Max ; Penfold, Christopher N ; James, Richard</creatorcontrib><description>Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA₁₋₁₀₇) of the translocation domain of colicin A (ColA) and TolB identified the TolB box as a 12-residue peptide that folded into a distorted hairpin within a central canyon of the β-propeller domain of TolB. Comparison of this structure with that of the colicin E9 (ColE9) TolB box-TolB complex, together with site-directed mutagenesis of the ColA TolB box residues, revealed important differences in the interaction of the two TolB boxes with an overlapping binding site on TolB. Substitution of the TolB box residues of ColA with those of ColE9 conferred the ability to competitively recruit TolB from Pal but reduced the biological activity of the mutant ColA. This datum explains (i) the difference in binding affinities of ColA and ColE9 with TolB, and (ii) the inability of ColA, unlike ColE9, to competitively recruit TolB from Pal, allowing an understanding of how these two colicins interact in a different way with a common translocation portal in E. coli cells.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2009.06808.x</identifier><identifier>PMID: 19627502</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Binding Sites ; Biological and medical sciences ; Cells ; Colicins - chemistry ; Colicins - genetics ; Colicins - metabolism ; Crystal structure ; Crystallography, X-Ray ; E coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Peptides ; Periplasmic Proteins - chemistry ; Periplasmic Proteins - metabolism ; Protein Transport ; Proteins</subject><ispartof>Molecular microbiology, 2010-02, Vol.75 (3), p.623-636</ispartof><rights>2009 The Authors. Journal compilation © 2009 Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Ltd. Feb 2010</rights><rights>Journal compilation © 2010 Blackwell Publishing</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5228-b1535593066c8403f16b479e366bf19a88ea5eb1c73161876dc459aedb9db2573</citedby><cites>FETCH-LOGICAL-c5228-b1535593066c8403f16b479e366bf19a88ea5eb1c73161876dc459aedb9db2573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.2009.06808.x$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2009.06808.x$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,27903,27904,45553,45554,46387,46811</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22318837$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19627502$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Ying</creatorcontrib><creatorcontrib>Li, Chan</creatorcontrib><creatorcontrib>Vankemmelbeke, Mireille N</creatorcontrib><creatorcontrib>Bardelang, Philip</creatorcontrib><creatorcontrib>Paoli, Max</creatorcontrib><creatorcontrib>Penfold, Christopher N</creatorcontrib><creatorcontrib>James, Richard</creatorcontrib><title>crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA₁₋₁₀₇) of the translocation domain of colicin A (ColA) and TolB identified the TolB box as a 12-residue peptide that folded into a distorted hairpin within a central canyon of the β-propeller domain of TolB. Comparison of this structure with that of the colicin E9 (ColE9) TolB box-TolB complex, together with site-directed mutagenesis of the ColA TolB box residues, revealed important differences in the interaction of the two TolB boxes with an overlapping binding site on TolB. Substitution of the TolB box residues of ColA with those of ColE9 conferred the ability to competitively recruit TolB from Pal but reduced the biological activity of the mutant ColA. This datum explains (i) the difference in binding affinities of ColA and ColE9 with TolB, and (ii) the inability of ColA, unlike ColE9, to competitively recruit TolB from Pal, allowing an understanding of how these two colicins interact in a different way with a common translocation portal in E. coli cells.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cells</subject><subject>Colicins - chemistry</subject><subject>Colicins - genetics</subject><subject>Colicins - metabolism</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>E coli</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Peptides</subject><subject>Periplasmic Proteins - chemistry</subject><subject>Periplasmic Proteins - metabolism</subject><subject>Protein Transport</subject><subject>Proteins</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>EIF</sourceid><recordid>eNqNUstu1DAUtRCIDoVfAAuJZYIf48RegNRWFCq1YkErsbMcx5nxKImD7bQzH8b_1WmiAXZk4cS55-WcAAAxynG6Pu5yTAuWEcF4ThASOSo44vn-GVgdB8_BCgmGMsrJzxPwKoQdQpiigr4EJ1gUpGSIrMBv7Q8hqhaG6EcdR2-ga2DcGnjr2nNYuf2016612vbwDKZFu25ozR4-2LidUd7cG9UGaLvB-aj6CGvbNMabXpswUSY9b7QfbexMGi8WSalz_awRvepD67SKNr160mnhGEwNqwPceDcOyX3JEV6DF00yNG-W-ym4u_xye_Etu_7-9eri7DrTjBCeVZhRxkQ6dKH5GtEGF9W6FIYWRdVgoTg3ipkK65LiAvOyqPWaCWXqStQVYSU9BZ9n3WGsOlPrlN2rVg7edsofpFNW_jvp7VZu3L0knGBGeBJ4vwh492s0IcqdG32fMsvUAcMIi3UC8RmkvQvBm-ZogJGc-pY7OdUqp1rl1Ld86lvuE_Xt3wH_EJeCE-DDAlBBq7ZJX1nbcMQRQjHndDrppxn3YFtz-O8A8ubmanpK_Hczv1FOqo1PHnc_yPTD4ZJwzjF9BF0-05k</recordid><startdate>201002</startdate><enddate>201002</enddate><creator>Zhang, Ying</creator><creator>Li, Chan</creator><creator>Vankemmelbeke, Mireille N</creator><creator>Bardelang, Philip</creator><creator>Paoli, Max</creator><creator>Penfold, Christopher N</creator><creator>James, Richard</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><scope>24P</scope><scope>IQODW</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>5PM</scope></search><sort><creationdate>201002</creationdate><title>crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins</title><author>Zhang, Ying ; Li, Chan ; Vankemmelbeke, Mireille N ; Bardelang, Philip ; Paoli, Max ; Penfold, Christopher N ; James, Richard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5228-b1535593066c8403f16b479e366bf19a88ea5eb1c73161876dc459aedb9db2573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cells</topic><topic>Colicins - chemistry</topic><topic>Colicins - genetics</topic><topic>Colicins - metabolism</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>E coli</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Peptides</topic><topic>Periplasmic Proteins - chemistry</topic><topic>Periplasmic Proteins - metabolism</topic><topic>Protein Transport</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Ying</creatorcontrib><creatorcontrib>Li, Chan</creatorcontrib><creatorcontrib>Vankemmelbeke, Mireille N</creatorcontrib><creatorcontrib>Bardelang, Philip</creatorcontrib><creatorcontrib>Paoli, Max</creatorcontrib><creatorcontrib>Penfold, Christopher N</creatorcontrib><creatorcontrib>James, Richard</creatorcontrib><collection>AGRIS</collection><collection>Wiley Online Library Open Access</collection><collection>Pascal-Francis</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>PubMed Central (Full Participant titles)</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Ying</au><au>Li, Chan</au><au>Vankemmelbeke, Mireille N</au><au>Bardelang, Philip</au><au>Paoli, Max</au><au>Penfold, Christopher N</au><au>James, Richard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2010-02</date><risdate>2010</risdate><volume>75</volume><issue>3</issue><spage>623</spage><epage>636</epage><pages>623-636</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA₁₋₁₀₇) of the translocation domain of colicin A (ColA) and TolB identified the TolB box as a 12-residue peptide that folded into a distorted hairpin within a central canyon of the β-propeller domain of TolB. Comparison of this structure with that of the colicin E9 (ColE9) TolB box-TolB complex, together with site-directed mutagenesis of the ColA TolB box residues, revealed important differences in the interaction of the two TolB boxes with an overlapping binding site on TolB. Substitution of the TolB box residues of ColA with those of ColE9 conferred the ability to competitively recruit TolB from Pal but reduced the biological activity of the mutant ColA. This datum explains (i) the difference in binding affinities of ColA and ColE9 with TolB, and (ii) the inability of ColA, unlike ColE9, to competitively recruit TolB from Pal, allowing an understanding of how these two colicins interact in a different way with a common translocation portal in E. coli cells.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19627502</pmid><doi>10.1111/j.1365-2958.2009.06808.x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0950-382X |
| ispartof | Molecular microbiology, 2010-02, Vol.75 (3), p.623-636 |
| issn | 0950-382X 1365-2958 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2821528 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Binding Sites Biological and medical sciences Cells Colicins - chemistry Colicins - genetics Colicins - metabolism Crystal structure Crystallography, X-Ray E coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Microbiology Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Peptides Periplasmic Proteins - chemistry Periplasmic Proteins - metabolism Protein Transport Proteins |
| title | crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T04%3A09%3A43IST&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%20structure%20of%20the%20TolB%20box%20of%20colicin%20A%20in%20complex%20with%20TolB%20reveals%20important%20differences%20in%20the%20recruitment%20of%20the%20common%20TolB%20translocation%20portal%20used%20by%20group%20A%20colicins&rft.jtitle=Molecular%20microbiology&rft.au=Zhang,%20Ying&rft.date=2010-02&rft.volume=75&rft.issue=3&rft.spage=623&rft.epage=636&rft.pages=623-636&rft.issn=0950-382X&rft.eissn=1365-2958&rft_id=info:doi/10.1111/j.1365-2958.2009.06808.x&rft_dat=%3Cproquest_pubme%3E1948283651%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=196510194&rft_id=info:pmid/19627502&rfr_iscdi=true |