Enhanced internal dynamics of a membrane transport protein during substrate translocation
Conformational changes are essential for the activity of many proteins. If, or how fast, internal fluctuations are related to slow conformational changes that mediate protein function is not understood. In this study, we measure internal fluctuations of the transport protein lactose permease in the...
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| Veröffentlicht in: | Protein science 2000-11, Vol.9 (11), p.2246-2250 |
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| container_title | Protein science |
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| creator | DÖRING, KLAUS SURREY, THOMAS GRÜNEWALD, SYLVIA JOHN, EDGAR JÄHNIG, FRITZ |
| description | Conformational changes are essential for the activity
of many proteins. If, or how fast, internal fluctuations
are related to slow conformational changes that mediate
protein function is not understood. In this study, we measure
internal fluctuations of the transport protein lactose
permease in the presence and absence of substrate by tryptophan
fluorescence spectroscopy. We demonstrate that nanosecond
fluctuations of α-helices are enhanced when the enzyme
transports substrate. This correlates with previously published
kinetic data from transport measurements showing that millisecond
conformational transitions of the substrate-loaded carrier
are faster than those in the absence of substrate. These
findings corroborate the hypothesis of the hierarchical
model of protein dynamics that predicts that slow conformational
transitions are based on fast, thermally activated internal
motions. |
| doi_str_mv | 10.1110/ps.9.11.2246 |
| format | Article |
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of many proteins. If, or how fast, internal fluctuations
are related to slow conformational changes that mediate
protein function is not understood. In this study, we measure
internal fluctuations of the transport protein lactose
permease in the presence and absence of substrate by tryptophan
fluorescence spectroscopy. We demonstrate that nanosecond
fluctuations of α-helices are enhanced when the enzyme
transports substrate. This correlates with previously published
kinetic data from transport measurements showing that millisecond
conformational transitions of the substrate-loaded carrier
are faster than those in the absence of substrate. These
findings corroborate the hypothesis of the hierarchical
model of protein dynamics that predicts that slow conformational
transitions are based on fast, thermally activated internal
motions.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.9.11.2246</identifier><identifier>PMID: 11152135</identifier><language>eng</language><publisher>Bristol: Cambridge University Press</publisher><subject>Animals ; Anisotropy ; Cell Line ; Escherichia coli Proteins ; helix fluctuations ; Kinetics ; lactose permease ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - metabolism ; Models, Statistical ; Models, Theoretical ; Monosaccharide Transport Proteins ; nanosecond motions ; Photons ; Protein Conformation ; protein dynamics ; Spectrometry, Fluorescence ; Symporters ; Time Factors ; time‐resolved tryptophan fluorescence anisotropy ; Tryptophan - chemistry</subject><ispartof>Protein science, 2000-11, Vol.9 (11), p.2246-2250</ispartof><rights>2000 The Protein Society</rights><rights>Copyright © 2000 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4616-ec64962db635dbb3aceb5232b4bfaca48ad702e7cfa7ced77444882696073c233</citedby><cites>FETCH-LOGICAL-c4616-ec64962db635dbb3aceb5232b4bfaca48ad702e7cfa7ced77444882696073c233</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/PMC2144487/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144487/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11152135$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DÖRING, KLAUS</creatorcontrib><creatorcontrib>SURREY, THOMAS</creatorcontrib><creatorcontrib>GRÜNEWALD, SYLVIA</creatorcontrib><creatorcontrib>JOHN, EDGAR</creatorcontrib><creatorcontrib>JÄHNIG, FRITZ</creatorcontrib><title>Enhanced internal dynamics of a membrane transport protein during substrate translocation</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>Conformational changes are essential for the activity
of many proteins. If, or how fast, internal fluctuations
are related to slow conformational changes that mediate
protein function is not understood. In this study, we measure
internal fluctuations of the transport protein lactose
permease in the presence and absence of substrate by tryptophan
fluorescence spectroscopy. We demonstrate that nanosecond
fluctuations of α-helices are enhanced when the enzyme
transports substrate. This correlates with previously published
kinetic data from transport measurements showing that millisecond
conformational transitions of the substrate-loaded carrier
are faster than those in the absence of substrate. These
findings corroborate the hypothesis of the hierarchical
model of protein dynamics that predicts that slow conformational
transitions are based on fast, thermally activated internal
motions.</description><subject>Animals</subject><subject>Anisotropy</subject><subject>Cell Line</subject><subject>Escherichia coli Proteins</subject><subject>helix fluctuations</subject><subject>Kinetics</subject><subject>lactose permease</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Models, Statistical</subject><subject>Models, Theoretical</subject><subject>Monosaccharide Transport Proteins</subject><subject>nanosecond motions</subject><subject>Photons</subject><subject>Protein Conformation</subject><subject>protein dynamics</subject><subject>Spectrometry, Fluorescence</subject><subject>Symporters</subject><subject>Time Factors</subject><subject>time‐resolved tryptophan fluorescence anisotropy</subject><subject>Tryptophan - chemistry</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1r3DAQxUVoaDZpbzkHnXqKN_qybF8CZdmmgYUNIYX2JCRZ3ijYkiPZCfvfV2ZN00LoRTMwPz09zQPgHKMlxhhd9XFZpW5JCONHYIEZr7Ky4j8_gAWqOM5KyssTcBrjE0KIYUI_gpN0MSeY5gvwa-0epdOmhtYNJjjZwnrvZGd1hL6BEnamU0E6A4d0xt6HAfbBD8Y6WI_Buh2Mo4ppOMxI67UcrHefwHEj22g-z_UM_Pi2flh9zzbbm9vV102mGcc8M5qzipNacZrXSlGpjcoJJYqpRmrJSlkXiJhCN7JINouCMVaWhFccFVQTSs_A9UG3H1Vnam1cstGKPthOhr3w0op_J84-ip1_EQRPUkUS-DILBP88mjiIzkZt2jb92o9RFCQnDOEJvDyAOvgYg2n-PIKRmLIQfRRV6sSURcIv_jb2Bs_LTwA-AK-2Nfv_iom7--0supw9yJSLrXdGPPlxyi2-7-I3MqimvQ</recordid><startdate>20001101</startdate><enddate>20001101</enddate><creator>DÖRING, KLAUS</creator><creator>SURREY, THOMAS</creator><creator>GRÜNEWALD, SYLVIA</creator><creator>JOHN, EDGAR</creator><creator>JÄHNIG, FRITZ</creator><general>Cambridge University Press</general><general>Cold Spring Harbor Laboratory Press</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20001101</creationdate><title>Enhanced internal dynamics of a membrane transport protein during substrate translocation</title><author>DÖRING, KLAUS ; SURREY, THOMAS ; GRÜNEWALD, SYLVIA ; JOHN, EDGAR ; JÄHNIG, FRITZ</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4616-ec64962db635dbb3aceb5232b4bfaca48ad702e7cfa7ced77444882696073c233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Anisotropy</topic><topic>Cell Line</topic><topic>Escherichia coli Proteins</topic><topic>helix fluctuations</topic><topic>Kinetics</topic><topic>lactose permease</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Models, Statistical</topic><topic>Models, Theoretical</topic><topic>Monosaccharide Transport Proteins</topic><topic>nanosecond motions</topic><topic>Photons</topic><topic>Protein Conformation</topic><topic>protein dynamics</topic><topic>Spectrometry, Fluorescence</topic><topic>Symporters</topic><topic>Time Factors</topic><topic>time‐resolved tryptophan fluorescence anisotropy</topic><topic>Tryptophan - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DÖRING, KLAUS</creatorcontrib><creatorcontrib>SURREY, THOMAS</creatorcontrib><creatorcontrib>GRÜNEWALD, SYLVIA</creatorcontrib><creatorcontrib>JOHN, EDGAR</creatorcontrib><creatorcontrib>JÄHNIG, FRITZ</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DÖRING, KLAUS</au><au>SURREY, THOMAS</au><au>GRÜNEWALD, SYLVIA</au><au>JOHN, EDGAR</au><au>JÄHNIG, FRITZ</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhanced internal dynamics of a membrane transport protein during substrate translocation</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2000-11-01</date><risdate>2000</risdate><volume>9</volume><issue>11</issue><spage>2246</spage><epage>2250</epage><pages>2246-2250</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>Conformational changes are essential for the activity
of many proteins. If, or how fast, internal fluctuations
are related to slow conformational changes that mediate
protein function is not understood. In this study, we measure
internal fluctuations of the transport protein lactose
permease in the presence and absence of substrate by tryptophan
fluorescence spectroscopy. We demonstrate that nanosecond
fluctuations of α-helices are enhanced when the enzyme
transports substrate. This correlates with previously published
kinetic data from transport measurements showing that millisecond
conformational transitions of the substrate-loaded carrier
are faster than those in the absence of substrate. These
findings corroborate the hypothesis of the hierarchical
model of protein dynamics that predicts that slow conformational
transitions are based on fast, thermally activated internal
motions.</abstract><cop>Bristol</cop><pub>Cambridge University Press</pub><pmid>11152135</pmid><doi>10.1110/ps.9.11.2246</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0961-8368 |
| ispartof | Protein science, 2000-11, Vol.9 (11), p.2246-2250 |
| issn | 0961-8368 1469-896X |
| language | eng |
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| source | MEDLINE; Wiley Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Anisotropy Cell Line Escherichia coli Proteins helix fluctuations Kinetics lactose permease Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Models, Statistical Models, Theoretical Monosaccharide Transport Proteins nanosecond motions Photons Protein Conformation protein dynamics Spectrometry, Fluorescence Symporters Time Factors time‐resolved tryptophan fluorescence anisotropy Tryptophan - chemistry |
| title | Enhanced internal dynamics of a membrane transport protein during substrate translocation |
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