Crystal Structure of Activated HutP: An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis
HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization ( hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on the hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; th...
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| Veröffentlicht in: | Structure (London) 2004-07, Vol.12 (7), p.1269-1280 |
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| creator | Kumarevel, Thirumananseri Fujimoto, Zui Karthe, Ponnuraj Oda, Masanao Mizuno, Hiroshi Kumar, Penmetcha K.R |
| description | HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (
hut) operon in
Bacillus subtilis by binding to
cis-acting regulatory sequences on the
hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel β strands in the central region of each monomer, with two α helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in
hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified. |
| doi_str_mv | 10.1016/j.str.2004.05.005 |
| format | Article |
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hut) operon in
Bacillus subtilis by binding to
cis-acting regulatory sequences on the
hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel β strands in the central region of each monomer, with two α helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in
hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2004.05.005</identifier><identifier>PMID: 15242603</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Bacillus subtilis ; Bacillus subtilis - genetics ; Bacillus subtilis - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; Crystallography, X-Ray ; Data Collection ; DNA Mutational Analysis ; Gene Expression Regulation, Bacterial ; Histidine - metabolism ; Models, Molecular ; Molecular Sequence Data ; Operon ; Protein Conformation ; RNA, Messenger - metabolism ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Transcription, Genetic</subject><ispartof>Structure (London), 2004-07, Vol.12 (7), p.1269-1280</ispartof><rights>2004 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.str.2004.05.005$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15242603$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kumarevel, Thirumananseri</creatorcontrib><creatorcontrib>Fujimoto, Zui</creatorcontrib><creatorcontrib>Karthe, Ponnuraj</creatorcontrib><creatorcontrib>Oda, Masanao</creatorcontrib><creatorcontrib>Mizuno, Hiroshi</creatorcontrib><creatorcontrib>Kumar, Penmetcha K.R</creatorcontrib><title>Crystal Structure of Activated HutP: An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis</title><title>Structure (London)</title><addtitle>Structure</addtitle><description>HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (
hut) operon in
Bacillus subtilis by binding to
cis-acting regulatory sequences on the
hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel β strands in the central region of each monomer, with two α helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in
hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.</description><subject>Amino Acid Sequence</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - genetics</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>Data Collection</subject><subject>DNA Mutational Analysis</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Histidine - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Operon</subject><subject>Protein Conformation</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Transcription, Genetic</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EokvhB3BBPnFLOrYTx4HTdlUoUkWrUs6W44y7XmWTxR-VeuKv41XbM6eRZp55pZmHkI8MagZMnu3qmELNAZoa2hqgfUVWTHWqapiSr8kKetlXnHF5Qt7FuAMA3gK8JSes5Q2XIFbk7yY8xmQm-iuFbFMOSBdH1zb5B5NwpJc53Xyh65ne_lzTcz-Pfr6nN2FJ6GeatibRW7zPU2EjvQtmjjb4Q_LLfIxJW6TbnOj1AUPplI1zY_005UhjHpKffHxP3jgzRfzwXE_J728Xd5vL6ur6-4_N-qpC3kOqOt66QfZWyM613FnetY3lpkE-jAJRMbROqMFy66BMemdVi40DlJ0YlOLilHx-yj2E5U_GmPTeR4vTZGZcctRSyp6J_v8gUyA6KVQBPz2DedjjqA_B70141C-_LcDXJwDLXQ8eg47W42xx9AFt0uPiNQN9NKl3upjUR5MaWl1Min_WjZGx</recordid><startdate>20040701</startdate><enddate>20040701</enddate><creator>Kumarevel, Thirumananseri</creator><creator>Fujimoto, Zui</creator><creator>Karthe, Ponnuraj</creator><creator>Oda, Masanao</creator><creator>Mizuno, Hiroshi</creator><creator>Kumar, Penmetcha K.R</creator><general>Elsevier Inc</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>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20040701</creationdate><title>Crystal Structure of Activated HutP: An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis</title><author>Kumarevel, Thirumananseri ; Fujimoto, Zui ; Karthe, Ponnuraj ; Oda, Masanao ; Mizuno, Hiroshi ; Kumar, Penmetcha K.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e290t-725fb69c367f52fc2754c2a4e2bd3ee81ecf38bc2cf054c9fc85e4f0e673b8823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - genetics</topic><topic>Bacillus subtilis - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>Data Collection</topic><topic>DNA Mutational Analysis</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Histidine - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Operon</topic><topic>Protein Conformation</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kumarevel, Thirumananseri</creatorcontrib><creatorcontrib>Fujimoto, Zui</creatorcontrib><creatorcontrib>Karthe, Ponnuraj</creatorcontrib><creatorcontrib>Oda, Masanao</creatorcontrib><creatorcontrib>Mizuno, Hiroshi</creatorcontrib><creatorcontrib>Kumar, Penmetcha K.R</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kumarevel, Thirumananseri</au><au>Fujimoto, Zui</au><au>Karthe, Ponnuraj</au><au>Oda, Masanao</au><au>Mizuno, Hiroshi</au><au>Kumar, Penmetcha K.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of Activated HutP: An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2004-07-01</date><risdate>2004</risdate><volume>12</volume><issue>7</issue><spage>1269</spage><epage>1280</epage><pages>1269-1280</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (
hut) operon in
Bacillus subtilis by binding to
cis-acting regulatory sequences on the
hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel β strands in the central region of each monomer, with two α helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in
hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15242603</pmid><doi>10.1016/j.str.2004.05.005</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Open Access: Cell Press Free Archives; Elsevier ScienceDirect Journals Collection; Free E-Journal (出版社公開部分のみ）; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Bacillus subtilis Bacillus subtilis - genetics Bacillus subtilis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Crystallography, X-Ray Data Collection DNA Mutational Analysis Gene Expression Regulation, Bacterial Histidine - metabolism Models, Molecular Molecular Sequence Data Operon Protein Conformation RNA, Messenger - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Transcription, Genetic |
| title | Crystal Structure of Activated HutP: An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis |
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