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Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA
Temperate bacteriophages are known for their bistability, which in TP901‐1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N‐terminal helix‐turn‐helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigat...
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Published in: | FEBS letters 2018-05, Vol.592 (10), p.1738-1750 |
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creator | Rasmussen, Kim K. Varming, Anders K. Schmidt, Simon N. Frandsen, Kristian E. H. Thulstrup, Peter W. Jensen, Malene Ringkjøbing Lo Leggio, Leila |
description | Temperate bacteriophages are known for their bistability, which in TP901‐1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N‐terminal helix‐turn‐helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high‐affinity binding to DNA. The crystal structure of the dimerization region (CTD1) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI‐NTD and small angle X‐ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix. |
doi_str_mv | 10.1002/1873-3468.13060 |
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This newly determined structure is used together with the known crystal structure of the CI‐NTD and small angle X‐ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.13060</identifier><identifier>PMID: 29683476</identifier><language>eng</language><publisher>England: Wiley</publisher><subject>Biochemistry, Molecular Biology ; dimerization domain ; helical hook motif ; Life Sciences ; phage repressor ; protein–DNA complex ; Structural Biology ; transcription factor</subject><ispartof>FEBS letters, 2018-05, Vol.592 (10), p.1738-1750</ispartof><rights>2018 Federation of European Biochemical Societies</rights><rights>2018 Federation of European Biochemical Societies.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-5135-0882 ; 0000-0003-0419-2196 ; 0000-0002-7136-9820</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29683476$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01995906$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Rasmussen, Kim K.</creatorcontrib><creatorcontrib>Varming, Anders K.</creatorcontrib><creatorcontrib>Schmidt, Simon N.</creatorcontrib><creatorcontrib>Frandsen, Kristian E. 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This newly determined structure is used together with the known crystal structure of the CI‐NTD and small angle X‐ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.</description><subject>Biochemistry, Molecular Biology</subject><subject>dimerization domain</subject><subject>helical hook motif</subject><subject>Life Sciences</subject><subject>phage repressor</subject><subject>protein–DNA complex</subject><subject>Structural Biology</subject><subject>transcription factor</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNo9kcFO20AQhlcVVUlDz72hPcLBdMZjr3ePIRCCFLWVGs6rTbzGWzlxumuD4NRH4Bn7JF0TyGnmn_lmDv_P2FeECwRIv6EsKKFMyAskEPCBjQ6TIzYCwCzJC0XH7HMIvyFqieoTO06VkJQVYsRWvzrfr7vem4avTHCBtxXvahvFurPetbva3Fu-_KkA__19QT695d7uvA2h9bx0m8g8m861W262JXfbeBQvB_3ouppffZ-csI-VaYL98lbH7G52vZzOk8WPm9vpZJHURARJXmVFXqR5KqwgElhVBRLmICuSmBJlmCuZ5pUqJZYVmoIKuQarMmVWCg3SmJ3v_9am0TvvNsY_6dY4PZ8s9DADVCpXIB4G9mzP7nz7p7eh0xsX1rZpzNa2fdApRIuy6BZE9PQN7VcbWx4-v3sYAbEHHl1jnw57BD1EpIdA9BCIfo1Iz64v09eO_gPCkYBC</recordid><startdate>201805</startdate><enddate>201805</enddate><creator>Rasmussen, Kim K.</creator><creator>Varming, Anders K.</creator><creator>Schmidt, Simon N.</creator><creator>Frandsen, Kristian E. 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H.</creatorcontrib><creatorcontrib>Thulstrup, Peter W.</creatorcontrib><creatorcontrib>Jensen, Malene Ringkjøbing</creatorcontrib><creatorcontrib>Lo Leggio, Leila</creatorcontrib><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rasmussen, Kim K.</au><au>Varming, Anders K.</au><au>Schmidt, Simon N.</au><au>Frandsen, Kristian E. 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The crystal structure of the dimerization region (CTD1) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI‐NTD and small angle X‐ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.</abstract><cop>England</cop><pub>Wiley</pub><pmid>29683476</pmid><doi>10.1002/1873-3468.13060</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-5135-0882</orcidid><orcidid>https://orcid.org/0000-0003-0419-2196</orcidid><orcidid>https://orcid.org/0000-0002-7136-9820</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Biochemistry, Molecular Biology dimerization domain helical hook motif Life Sciences phage repressor protein–DNA complex Structural Biology transcription factor |
title | Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA |
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