Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator
Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and...
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| Veröffentlicht in: | PloS one 2011-05, Vol.6 (5), p.e19529 |
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| description | Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR. |
| doi_str_mv | 10.1371/journal.pone.0019529 |
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RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0019529</identifier><identifier>PMID: 21559286</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Automation ; Binding ; Biology ; Biophysics ; Catabolism ; Chemical bonds ; Corynebacterium glutamicum ; Corynebacterium glutamicum - metabolism ; Crystal structure ; Crystallography ; Crystallography, X-Ray - methods ; Data collection ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; Gene Expression Regulation, Bacterial ; Genetic aspects ; Helices ; Homology ; Hydrogen ; Hydrogen bonding ; Hydrogen bonds ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Laboratories ; Ligands ; Microbial drug resistance ; Models, Molecular ; Molecular Conformation ; Molecular Sequence Data ; Multidrug resistance ; Mutagenesis ; Mutagenesis, Site-Directed ; Pathogenicity ; Pathogens ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Proteins ; Recognition ; Residues ; Resorcinol ; Resorcinols - pharmacology ; Sequence Homology, Amino Acid ; Structure-function relationships ; Transcription ; Transcription (Genetics) ; Transcription, Genetic ; Water - chemistry</subject><ispartof>PloS one, 2011-05, Vol.6 (5), p.e19529</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Li et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Li et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6069-b6ca5c8b84bb04b0b39713c768489ecf60bc97d6eceb0caedfde2cf4bf73b6ff3</citedby><cites>FETCH-LOGICAL-c6069-b6ca5c8b84bb04b0b39713c768489ecf60bc97d6eceb0caedfde2cf4bf73b6ff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086911/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086911/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21559286$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Xu, Wenqing</contributor><creatorcontrib>Li, De-Feng</creatorcontrib><creatorcontrib>Zhang, Ning</creatorcontrib><creatorcontrib>Hou, Yan-Jie</creatorcontrib><creatorcontrib>Huang, Yan</creatorcontrib><creatorcontrib>Hu, Yonglin</creatorcontrib><creatorcontrib>Zhang, Ying</creatorcontrib><creatorcontrib>Liu, Shuang-Jiang</creatorcontrib><creatorcontrib>Wang, Da-Cheng</creatorcontrib><title>Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Automation</subject><subject>Binding</subject><subject>Biology</subject><subject>Biophysics</subject><subject>Catabolism</subject><subject>Chemical bonds</subject><subject>Corynebacterium glutamicum</subject><subject>Corynebacterium glutamicum - metabolism</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray - methods</subject><subject>Data collection</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genetic aspects</subject><subject>Helices</subject><subject>Homology</subject><subject>Hydrogen</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Laboratories</subject><subject>Ligands</subject><subject>Microbial drug resistance</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Molecular Sequence Data</subject><subject>Multidrug resistance</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Recognition</subject><subject>Residues</subject><subject>Resorcinol</subject><subject>Resorcinols - pharmacology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-function relationships</subject><subject>Transcription</subject><subject>Transcription (Genetics)</subject><subject>Transcription, Genetic</subject><subject>Water - chemistry</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNktuL1DAUxoso7jr6H4gWBMGHGZNe0uZFWAYvAwsL4-U1JOlJJ0ObjEk6uuAfb-p0lykoSB5yOb_znfDxJclzjFY4r_DbvR2c4d3qYA2sEMK0zOiD5BLTPFuSDOUPz84XyRPv9wiVeU3I4-Qiw2VJs5pcJr_W7tYH3qU-uEGGwYFPrUrDDtLguPHS6UPQNg5KHRxi1VuXbm23jdcj8M6nPDX2CGNZ2tboEU57kDtutO9TAeEHgEm1aQYJLuWmiWQ7dDxY9zR5pKIEPJv2RfL1w_sv60_L65uPm_XV9VISROhSEMlLWYu6EAIVAomcVjiXFamLmoJUBAlJq4aABIEkh0Y1kElVCFXlgiiVL5KXJ91DZz2bjPMMZ7So6wqXKBKbE9FYvmcHp3vubpnlmv15sK5l3AUtO2C0yOroXVWguMbZFBPFScUFyLKMFi-Sd9O0QfTQSDDRyW4mOq8YvWOtPbIc1YRiHAVeTQLOfh_Ah398eaJaHn-ljbJRTPbaS3ZVRG9oFm2K1OovVFwN9FrG6Cgd32cNb2YNkQnwM7R88J5tPm__n735Nmdfn7G7GJ2w87Ybxrz4OVicQOms9w7UvXMYsTH5d26wMflsSn5se3Hu-n3TXdTz30YcAmI</recordid><startdate>20110503</startdate><enddate>20110503</enddate><creator>Li, De-Feng</creator><creator>Zhang, Ning</creator><creator>Hou, Yan-Jie</creator><creator>Huang, Yan</creator><creator>Hu, Yonglin</creator><creator>Zhang, Ying</creator><creator>Liu, Shuang-Jiang</creator><creator>Wang, Da-Cheng</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110503</creationdate><title>Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator</title><author>Li, De-Feng ; Zhang, Ning ; Hou, Yan-Jie ; Huang, Yan ; Hu, Yonglin ; Zhang, Ying ; Liu, Shuang-Jiang ; Wang, Da-Cheng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6069-b6ca5c8b84bb04b0b39713c768489ecf60bc97d6eceb0caedfde2cf4bf73b6ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Automation</topic><topic>Binding</topic><topic>Biology</topic><topic>Biophysics</topic><topic>Catabolism</topic><topic>Chemical bonds</topic><topic>Corynebacterium glutamicum</topic><topic>Corynebacterium glutamicum - 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RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21559286</pmid><doi>10.1371/journal.pone.0019529</doi><tpages>e19529</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | PloS one, 2011-05, Vol.6 (5), p.e19529 |
| issn | 1932-6203 1932-6203 |
| language | eng |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Amino Acid Motifs Amino Acid Sequence Automation Binding Biology Biophysics Catabolism Chemical bonds Corynebacterium glutamicum Corynebacterium glutamicum - metabolism Crystal structure Crystallography Crystallography, X-Ray - methods Data collection Deoxyribonucleic acid DNA DNA - chemistry Gene Expression Regulation, Bacterial Genetic aspects Helices Homology Hydrogen Hydrogen bonding Hydrogen bonds Hydrophobic and Hydrophilic Interactions Hydrophobicity Laboratories Ligands Microbial drug resistance Models, Molecular Molecular Conformation Molecular Sequence Data Multidrug resistance Mutagenesis Mutagenesis, Site-Directed Pathogenicity Pathogens Protein Binding Protein Conformation Protein Structure, Tertiary Proteins Recognition Residues Resorcinol Resorcinols - pharmacology Sequence Homology, Amino Acid Structure-function relationships Transcription Transcription (Genetics) Transcription, Genetic Water - chemistry |
| title | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T10%3A35%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structures%20of%20the%20transcriptional%20repressor%20RolR%20reveals%20a%20novel%20recognition%20mechanism%20between%20inducer%20and%20regulator&rft.jtitle=PloS%20one&rft.au=Li,%20De-Feng&rft.date=2011-05-03&rft.volume=6&rft.issue=5&rft.spage=e19529&rft.pages=e19529-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0019529&rft_dat=%3Cgale_plos_%3EA476892397%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1294887150&rft_id=info:pmid/21559286&rft_galeid=A476892397&rft_doaj_id=oai_doaj_org_article_9428928740404f60b916fa67abec5505&rfr_iscdi=true |