Two-State Allosteric Behavior in a Single-Domain Signaling Protein
Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we charac...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2001-03, Vol.291 (5512), p.2429-2433 |
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| creator | Volkman, Brian F. Lipson, Doron Wemmer, David E. Kern, Dorothee |
| description | Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation. |
| doi_str_mv | 10.1126/science.291.5512.2429 |
| format | Article |
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We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.291.5512.2429</identifier><identifier>PMID: 11264542</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Allosteric Regulation ; Amides ; Bacterial Proteins ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Cell physiology ; Cellular signal transduction ; Chemical equilibrium ; Conformation ; Correlations ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Modeling ; Models, Molecular ; Molecular and cellular biology ; Motion ; Mutation ; NMR ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; PII Nitrogen Regulatory Proteins ; Population dynamics ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Rotation ; Signal Transduction ; Time ; Trans-Activators ; Transcription Factors</subject><ispartof>Science (American Association for the Advancement of Science), 2001-03, Vol.291 (5512), p.2429-2433</ispartof><rights>Copyright 2001 American Association for the Advancement of Science</rights><rights>2001 INIST-CNRS</rights><rights>COPYRIGHT 2001 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2001 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Mar 23, 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c754t-27784f6715f5a7cd164a25b5197572d76c9052d0d69de3550c2a0a1415badc8c3</citedby><cites>FETCH-LOGICAL-c754t-27784f6715f5a7cd164a25b5197572d76c9052d0d69de3550c2a0a1415badc8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3082688$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3082688$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=990996$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11264542$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Volkman, Brian F.</creatorcontrib><creatorcontrib>Lipson, Doron</creatorcontrib><creatorcontrib>Wemmer, David E.</creatorcontrib><creatorcontrib>Kern, Dorothee</creatorcontrib><title>Two-State Allosteric Behavior in a Single-Domain Signaling Protein</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.</description><subject>Allosteric Regulation</subject><subject>Amides</subject><subject>Bacterial Proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>Cellular signal transduction</subject><subject>Chemical equilibrium</subject><subject>Conformation</subject><subject>Correlations</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Modeling</subject><subject>Models, Molecular</subject><subject>Molecular and cellular biology</subject><subject>Motion</subject><subject>Mutation</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Phosphorylation</subject><subject>PII Nitrogen Regulatory Proteins</subject><subject>Population dynamics</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Rotation</subject><subject>Signal Transduction</subject><subject>Time</subject><subject>Trans-Activators</subject><subject>Transcription Factors</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0l2LEzEUBuBBFLe7-g9UhhXUi52aZPIxuWyr1oViha7ehjRzZkxJJ2syXfXfm9qyUilSchGS8yQhnDfLnmM0xJjwt9FY6AwMicRDxjAZEkrkg2yAkWSFJKh8mA0QKnlRIcHOsvMYVwilmiwfZ2fbGyijZJCNb374YtHrHvKRcz72EKzJx_BN31kfctvlOl_YrnVQvPNrndYL23bapa38c_A92O5J9qjRLsLT_XyRffnw_mbysZjNp9eT0awwgtG-IEJUtOECs4ZpYWrMqSZsybAUTJBacCMRIzWquayhZAwZopHGFLOlrk1lyovs1e7e2-C_byD2am2jAed0B34TleBSEsbKBF__H9Iy_Z3zKsnLf-TKb0L6XlQEl0xIKmlCVzvUagfKdo3vgzYtdBC08x00Nm2PBKl4RSVPvDjC06hhbc0x_-bAJ9LDz77VmxjV9eLTyXT-9WQ6np5Kq-nsgF4do8Y7By2o1O7J_ICzHTfBxxigUbfBrnX4pTBS2wyqfYpVSrHaplhtU5zOvdi3ZbNcQ_331D62CbzcAx2Ndk3QnbHx3kmJ5J_nn-3UKvY-3FdLVBFeVeVvPDP-Cw</recordid><startdate>20010323</startdate><enddate>20010323</enddate><creator>Volkman, Brian F.</creator><creator>Lipson, Doron</creator><creator>Wemmer, David E.</creator><creator>Kern, Dorothee</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010323</creationdate><title>Two-State Allosteric Behavior in a Single-Domain Signaling Protein</title><author>Volkman, Brian F. ; 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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2001-03, Vol.291 (5512), p.2429-2433 |
| issn | 0036-8075 1095-9203 |
| language | eng |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Allosteric Regulation Amides Bacterial Proteins Binding Sites Biochemistry Biological and medical sciences Cell physiology Cellular signal transduction Chemical equilibrium Conformation Correlations DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Modeling Models, Molecular Molecular and cellular biology Motion Mutation NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Phosphorylation PII Nitrogen Regulatory Proteins Population dynamics Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Proteins Rotation Signal Transduction Time Trans-Activators Transcription Factors |
| title | Two-State Allosteric Behavior in a Single-Domain Signaling Protein |
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