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Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein
The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upo...
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Published in: | International journal of biological macromolecules 2012-01, Vol.50 (1), p.1-6 |
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creator | Gao, Zhengya Li, Feng Wu, Guangrong Zhu, Yanrun Yu, Ting Yu, Shaoning |
description | The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission. |
doi_str_mv | 10.1016/j.ijbiomac.2011.08.016 |
format | article |
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In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2011.08.016</identifier><identifier>PMID: 21889533</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>adenosine monophosphate ; Amino Acid Motifs ; Calorimetry - methods ; cAMP ; cAMP binding motif ; cAMP receptor protein ; Chymotrypsin - chemistry ; Circular Dichroism ; Conformational change ; cyclic AMP ; Cyclic AMP Receptor Protein - chemistry ; Cyclic AMP Receptor Protein - metabolism ; Dimerization ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; genes ; Kinetics ; Macromolecular Substances - chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Signal Transduction ; Spectrometry, Fluorescence - methods ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Temperature</subject><ispartof>International journal of biological macromolecules, 2012-01, Vol.50 (1), p.1-6</ispartof><rights>2011 Elsevier B.V.</rights><rights>Copyright © 2011 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-6f83a12572ff77c662f097635483da5d187b8950c65f910dc777bec78de716c73</citedby><cites>FETCH-LOGICAL-c391t-6f83a12572ff77c662f097635483da5d187b8950c65f910dc777bec78de716c73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4009,27902,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21889533$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gao, Zhengya</creatorcontrib><creatorcontrib>Li, Feng</creatorcontrib><creatorcontrib>Wu, Guangrong</creatorcontrib><creatorcontrib>Zhu, Yanrun</creatorcontrib><creatorcontrib>Yu, Ting</creatorcontrib><creatorcontrib>Yu, Shaoning</creatorcontrib><title>Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.</description><subject>adenosine monophosphate</subject><subject>Amino Acid Motifs</subject><subject>Calorimetry - methods</subject><subject>cAMP</subject><subject>cAMP binding motif</subject><subject>cAMP receptor protein</subject><subject>Chymotrypsin - chemistry</subject><subject>Circular Dichroism</subject><subject>Conformational change</subject><subject>cyclic AMP</subject><subject>Cyclic AMP Receptor Protein - chemistry</subject><subject>Cyclic AMP Receptor Protein - metabolism</subject><subject>Dimerization</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>genes</subject><subject>Kinetics</subject><subject>Macromolecular Substances - chemistry</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Signal Transduction</subject><subject>Spectrometry, Fluorescence - methods</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Temperature</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNqFkMFOGzEQhq2KqqS0r0B948JuPeus7b2BEJRKVK2gnC1ndpw42qyDvUHi7esowLUnS6Pv_2f8MXYKogYB6vu6DutFiBuHdSMAamHqMv7AZmB0Vwkh5BGbCZhDZUCKY_Y553WZqhbMJ3bcgDFdK-WM-fs4UObR81UYl8QTLUMcz_kQ4zZzyd3Y8zkPI59WxB1O4dlNBdgHrjOuKAVcBccxDoHjCw4B-eWvP6UGaTvFxLcpThTGL-yjd0Omr6_vCXu8uf57dVvd_f7x8-ryrkLZwVQpb6SDptWN91qjUo0XnVaynRvZu7Yvn1uUwwWq1ncgetRaLwi16UmDQi1P2Nmht-x92lGe7CZkpGFwI8Vdth00UBqNLKQ6kJhizom83aawcenFgrB7xXZt3xTbvWIrjC3jEjx9XbFbbKh_j705LcC3A-BdtG6ZQraPD6VBFf-tUUoU4uJAUFHxHCjZjIFGpD4UcZPtY_jfFf8AQuaYIA</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Gao, Zhengya</creator><creator>Li, Feng</creator><creator>Wu, Guangrong</creator><creator>Zhu, Yanrun</creator><creator>Yu, Ting</creator><creator>Yu, Shaoning</creator><general>Elsevier B.V</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>20120101</creationdate><title>Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein</title><author>Gao, Zhengya ; 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subjects | adenosine monophosphate Amino Acid Motifs Calorimetry - methods cAMP cAMP binding motif cAMP receptor protein Chymotrypsin - chemistry Circular Dichroism Conformational change cyclic AMP Cyclic AMP Receptor Protein - chemistry Cyclic AMP Receptor Protein - metabolism Dimerization Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - chemistry genes Kinetics Macromolecular Substances - chemistry Protein Binding Protein Conformation Protein Structure, Tertiary Signal Transduction Spectrometry, Fluorescence - methods Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Temperature |
title | Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein |
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