Dynamic Allostery in the Ring Protein TRAP
We have discovered distinct, characteristic differences in the thermodynamic signatures of tryptophan binding by trp RNA-binding attenuation protein (TRAP) from two different bacterial species. The TRAP 11mer ring binds 11 molecules of tryptophan at symmetry-related sites. Tryptophan binding to Baci...
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| Veröffentlicht in: | Journal of molecular biology 2007-08, Vol.371 (1), p.154-167 |
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| container_title | Journal of molecular biology |
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| creator | Heddle, Jonathan G. Okajima, Tomoyuki Scott, David J. Akashi, Satoko Park, Sam-Yong Tame, Jeremy R.H. |
| description | We have discovered distinct, characteristic differences in the thermodynamic signatures of tryptophan binding by
trp RNA-binding attenuation protein (TRAP) from two different bacterial species. The TRAP 11mer ring binds 11 molecules of tryptophan at symmetry-related sites. Tryptophan binding to
Bacillus stearothermophilus TRAP is not cooperative, but isothermal titration calorimetry shows that filling the first tryptophan binding sites of
Bacillus subtilis TRAP has a marked effect on the thermodynamics of subsequent ligand binding. We have identified a single, conservative amino acid replacement (Ile to Leu) in
B. subtilis TRAP that abolishes this effect, and suggest the initial ligand binding causes a change throughout the wild-type protein ring. |
| doi_str_mv | 10.1016/j.jmb.2007.05.013 |
| format | Article |
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trp RNA-binding attenuation protein (TRAP) from two different bacterial species. The TRAP 11mer ring binds 11 molecules of tryptophan at symmetry-related sites. Tryptophan binding to
Bacillus stearothermophilus TRAP is not cooperative, but isothermal titration calorimetry shows that filling the first tryptophan binding sites of
Bacillus subtilis TRAP has a marked effect on the thermodynamics of subsequent ligand binding. We have identified a single, conservative amino acid replacement (Ile to Leu) in
B. subtilis TRAP that abolishes this effect, and suggest the initial ligand binding causes a change throughout the wild-type protein ring.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2007.05.013</identifier><identifier>PMID: 17559872</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Allosteric Regulation ; Amino Acid Sequence ; Bacillus stearothermophilus ; Bacillus subtilis ; Bacillus subtilis - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Calorimetry ; conformation ; cooperativity ; Geobacillus stearothermophilus - metabolism ; isothermal titration calorimetry (ITC) ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; protein dynamics ; ring protein ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Sequence Alignment ; Thermodynamics ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Tryptophan - metabolism</subject><ispartof>Journal of molecular biology, 2007-08, Vol.371 (1), p.154-167</ispartof><rights>2007 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-bc0f5a3d61ac418a58ffa84d8bdcfcb4859e26102c7d8446dfe3d7381de3d9ee3</citedby><cites>FETCH-LOGICAL-c382t-bc0f5a3d61ac418a58ffa84d8bdcfcb4859e26102c7d8446dfe3d7381de3d9ee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2007.05.013$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17559872$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heddle, Jonathan G.</creatorcontrib><creatorcontrib>Okajima, Tomoyuki</creatorcontrib><creatorcontrib>Scott, David J.</creatorcontrib><creatorcontrib>Akashi, Satoko</creatorcontrib><creatorcontrib>Park, Sam-Yong</creatorcontrib><creatorcontrib>Tame, Jeremy R.H.</creatorcontrib><title>Dynamic Allostery in the Ring Protein TRAP</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>We have discovered distinct, characteristic differences in the thermodynamic signatures of tryptophan binding by
trp RNA-binding attenuation protein (TRAP) from two different bacterial species. The TRAP 11mer ring binds 11 molecules of tryptophan at symmetry-related sites. Tryptophan binding to
Bacillus stearothermophilus TRAP is not cooperative, but isothermal titration calorimetry shows that filling the first tryptophan binding sites of
Bacillus subtilis TRAP has a marked effect on the thermodynamics of subsequent ligand binding. We have identified a single, conservative amino acid replacement (Ile to Leu) in
B. subtilis TRAP that abolishes this effect, and suggest the initial ligand binding causes a change throughout the wild-type protein ring.</description><subject>Allosteric Regulation</subject><subject>Amino Acid Sequence</subject><subject>Bacillus stearothermophilus</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Calorimetry</subject><subject>conformation</subject><subject>cooperativity</subject><subject>Geobacillus stearothermophilus - metabolism</subject><subject>isothermal titration calorimetry (ITC)</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>protein dynamics</subject><subject>ring protein</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Thermodynamics</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Tryptophan - metabolism</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLw0AUhQdRbK3-ADeSlQsh8U4mk9zgqtQnFCylrodk5kan5KEzqdB_b0oL7nR14PCds_gYu-QQceDp7TpaN2UUA2QRyAi4OGJjDpiHmAo8ZmOAOA5jFOmInXm_BgApEjxlI55JmWMWj9nN_bYtGquDaV13vie3DWwb9B8ULG37Hixc19NQrJbTxTk7qYra08UhJ-zt8WE1ew7nr08vs-k81ALjPiw1VLIQJuWFTjgWEquqwMRgaXSlywRlTnHKIdaZwSRJTUXCZAK5GTInEhN2vf_9dN3XhnyvGus11XXRUrfxKoMMUOT8X5DnmAOXOIB8D2rXee-oUp_ONoXbKg5qZ1Kt1WBS7UwqkGowOWyuDuebsiHzuzioG4C7PUCDi29LTnltqdVkrCPdK9PZP-5_ADWqgmw</recordid><startdate>20070803</startdate><enddate>20070803</enddate><creator>Heddle, Jonathan G.</creator><creator>Okajima, Tomoyuki</creator><creator>Scott, David J.</creator><creator>Akashi, Satoko</creator><creator>Park, Sam-Yong</creator><creator>Tame, Jeremy R.H.</creator><general>Elsevier Ltd</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>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20070803</creationdate><title>Dynamic Allostery in the Ring Protein TRAP</title><author>Heddle, Jonathan G. ; Okajima, Tomoyuki ; Scott, David J. ; Akashi, Satoko ; Park, Sam-Yong ; Tame, Jeremy R.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-bc0f5a3d61ac418a58ffa84d8bdcfcb4859e26102c7d8446dfe3d7381de3d9ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Allosteric Regulation</topic><topic>Amino Acid Sequence</topic><topic>Bacillus stearothermophilus</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Calorimetry</topic><topic>conformation</topic><topic>cooperativity</topic><topic>Geobacillus stearothermophilus - metabolism</topic><topic>isothermal titration calorimetry (ITC)</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>protein dynamics</topic><topic>ring protein</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Thermodynamics</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Tryptophan - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heddle, Jonathan G.</creatorcontrib><creatorcontrib>Okajima, Tomoyuki</creatorcontrib><creatorcontrib>Scott, David J.</creatorcontrib><creatorcontrib>Akashi, Satoko</creatorcontrib><creatorcontrib>Park, Sam-Yong</creatorcontrib><creatorcontrib>Tame, Jeremy R.H.</creatorcontrib><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>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heddle, Jonathan G.</au><au>Okajima, Tomoyuki</au><au>Scott, David J.</au><au>Akashi, Satoko</au><au>Park, Sam-Yong</au><au>Tame, Jeremy R.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamic Allostery in the Ring Protein TRAP</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2007-08-03</date><risdate>2007</risdate><volume>371</volume><issue>1</issue><spage>154</spage><epage>167</epage><pages>154-167</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>We have discovered distinct, characteristic differences in the thermodynamic signatures of tryptophan binding by
trp RNA-binding attenuation protein (TRAP) from two different bacterial species. The TRAP 11mer ring binds 11 molecules of tryptophan at symmetry-related sites. Tryptophan binding to
Bacillus stearothermophilus TRAP is not cooperative, but isothermal titration calorimetry shows that filling the first tryptophan binding sites of
Bacillus subtilis TRAP has a marked effect on the thermodynamics of subsequent ligand binding. We have identified a single, conservative amino acid replacement (Ile to Leu) in
B. subtilis TRAP that abolishes this effect, and suggest the initial ligand binding causes a change throughout the wild-type protein ring.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>17559872</pmid><doi>10.1016/j.jmb.2007.05.013</doi><tpages>14</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 2007-08, Vol.371 (1), p.154-167 |
| issn | 0022-2836 1089-8638 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Allosteric Regulation Amino Acid Sequence Bacillus stearothermophilus Bacillus subtilis Bacillus subtilis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Calorimetry conformation cooperativity Geobacillus stearothermophilus - metabolism isothermal titration calorimetry (ITC) Models, Molecular Molecular Sequence Data Mutation Protein Binding Protein Conformation protein dynamics ring protein RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Sequence Alignment Thermodynamics Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Tryptophan - metabolism |
| title | Dynamic Allostery in the Ring Protein TRAP |
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