Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB
The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required...
Gespeichert in:
| Veröffentlicht in: | Journal of molecular biology 2006-03, Vol.357 (1), p.62-72 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 72 |
|---|---|
| container_issue | 1 |
| container_start_page | 62 |
| container_title | Journal of molecular biology |
| container_volume | 357 |
| creator | Eryilmaz, Jitka Ceschini, Simona Ryan, James Geddes, Stella Waters, Timothy R. Barrett, Tracey E. |
| description | The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the β-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the β-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase. |
| doi_str_mv | 10.1016/j.jmb.2005.12.059 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_17110937</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022283605016359</els_id><sourcerecordid>17110937</sourcerecordid><originalsourceid>FETCH-LOGICAL-c382t-e4e72db46379009d02cafb0572870b923d484a9eeb651bccc91503bbccac313a3</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwAWyQV-wSxnaeYlXKq6gCJNq15ThT6ihNiu1U6t-TqpXYsZq7OPdKcwi5ZhAyYMldFVbrIuQAcch4CHF-QoYMsjzIEpGdkiEA5wHPRDIgF85V0IMiys7JgCURTxIRDcnbl7ed9p1VNZ02znyvvKOm8S31K6QTu9t4o-nj-zgocYNNiY2n4_mnckjH2put8TvaLuliax8uydlS1Q6vjndEFs9P88lrMPt4mU7Gs0CLjPsAI0x5WUSJSHOAvASu1bKAOOVZCkXORRllkcoRiyRmhdY6ZzGIok9KCyaUGJHbw-7Gtj8dOi_Xxmmsa9Vg2znJUsYgF2kPsgOobeucxaXcWLNWdicZyL1AWcleoNwLlIzLXmDfuTmOd8Uay7_G0VgP3B8A7F_cGrTSaYONxtJY1F6Wrfln_hdr24Au</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17110937</pqid></control><display><type>article</type><title>Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Eryilmaz, Jitka ; Ceschini, Simona ; Ryan, James ; Geddes, Stella ; Waters, Timothy R. ; Barrett, Tracey E.</creator><creatorcontrib>Eryilmaz, Jitka ; Ceschini, Simona ; Ryan, James ; Geddes, Stella ; Waters, Timothy R. ; Barrett, Tracey E.</creatorcontrib><description>The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the β-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the β-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2005.12.059</identifier><identifier>PMID: 16426634</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adenosine Diphosphate - chemistry ; Adenosine Diphosphate - metabolism ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; ADP ; Bacillus - enzymology ; Bacillus - genetics ; Bacillus subtilis - chemistry ; Bacillus subtilis - enzymology ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; complex ; Crystallography, X-Ray ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA Helicases - chemistry ; DNA Helicases - genetics ; DNA Helicases - metabolism ; DNA Repair ; helicase ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermus thermophilus - enzymology ; Thermus thermophilus - genetics ; UvrB</subject><ispartof>Journal of molecular biology, 2006-03, Vol.357 (1), p.62-72</ispartof><rights>2005 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-e4e72db46379009d02cafb0572870b923d484a9eeb651bccc91503bbccac313a3</citedby><cites>FETCH-LOGICAL-c382t-e4e72db46379009d02cafb0572870b923d484a9eeb651bccc91503bbccac313a3</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.2005.12.059$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16426634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Eryilmaz, Jitka</creatorcontrib><creatorcontrib>Ceschini, Simona</creatorcontrib><creatorcontrib>Ryan, James</creatorcontrib><creatorcontrib>Geddes, Stella</creatorcontrib><creatorcontrib>Waters, Timothy R.</creatorcontrib><creatorcontrib>Barrett, Tracey E.</creatorcontrib><title>Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the β-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the β-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase.</description><subject>Adenosine Diphosphate - chemistry</subject><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>ADP</subject><subject>Bacillus - enzymology</subject><subject>Bacillus - genetics</subject><subject>Bacillus subtilis - chemistry</subject><subject>Bacillus subtilis - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>complex</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA Helicases - chemistry</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - metabolism</subject><subject>DNA Repair</subject><subject>helicase</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Thermus thermophilus - enzymology</subject><subject>Thermus thermophilus - genetics</subject><subject>UvrB</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EoqXwAWyQV-wSxnaeYlXKq6gCJNq15ThT6ihNiu1U6t-TqpXYsZq7OPdKcwi5ZhAyYMldFVbrIuQAcch4CHF-QoYMsjzIEpGdkiEA5wHPRDIgF85V0IMiys7JgCURTxIRDcnbl7ed9p1VNZ02znyvvKOm8S31K6QTu9t4o-nj-zgocYNNiY2n4_mnckjH2put8TvaLuliax8uydlS1Q6vjndEFs9P88lrMPt4mU7Gs0CLjPsAI0x5WUSJSHOAvASu1bKAOOVZCkXORRllkcoRiyRmhdY6ZzGIok9KCyaUGJHbw-7Gtj8dOi_Xxmmsa9Vg2znJUsYgF2kPsgOobeucxaXcWLNWdicZyL1AWcleoNwLlIzLXmDfuTmOd8Uay7_G0VgP3B8A7F_cGrTSaYONxtJY1F6Wrfln_hdr24Au</recordid><startdate>20060317</startdate><enddate>20060317</enddate><creator>Eryilmaz, Jitka</creator><creator>Ceschini, Simona</creator><creator>Ryan, James</creator><creator>Geddes, Stella</creator><creator>Waters, Timothy R.</creator><creator>Barrett, Tracey E.</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>7TM</scope></search><sort><creationdate>20060317</creationdate><title>Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB</title><author>Eryilmaz, Jitka ; Ceschini, Simona ; Ryan, James ; Geddes, Stella ; Waters, Timothy R. ; Barrett, Tracey E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-e4e72db46379009d02cafb0572870b923d484a9eeb651bccc91503bbccac313a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine Diphosphate - chemistry</topic><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>ADP</topic><topic>Bacillus - enzymology</topic><topic>Bacillus - genetics</topic><topic>Bacillus subtilis - chemistry</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>complex</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>DNA Helicases - chemistry</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - metabolism</topic><topic>DNA Repair</topic><topic>helicase</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Binding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Thermus thermophilus - enzymology</topic><topic>Thermus thermophilus - genetics</topic><topic>UvrB</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eryilmaz, Jitka</creatorcontrib><creatorcontrib>Ceschini, Simona</creatorcontrib><creatorcontrib>Ryan, James</creatorcontrib><creatorcontrib>Geddes, Stella</creatorcontrib><creatorcontrib>Waters, Timothy R.</creatorcontrib><creatorcontrib>Barrett, Tracey E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eryilmaz, Jitka</au><au>Ceschini, Simona</au><au>Ryan, James</au><au>Geddes, Stella</au><au>Waters, Timothy R.</au><au>Barrett, Tracey E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2006-03-17</date><risdate>2006</risdate><volume>357</volume><issue>1</issue><spage>62</spage><epage>72</epage><pages>62-72</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the β-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the β-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>16426634</pmid><doi>10.1016/j.jmb.2005.12.059</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 2006-03, Vol.357 (1), p.62-72 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_17110937 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism ADP Bacillus - enzymology Bacillus - genetics Bacillus subtilis - chemistry Bacillus subtilis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism complex Crystallography, X-Ray DNA DNA - chemistry DNA - metabolism DNA Helicases - chemistry DNA Helicases - genetics DNA Helicases - metabolism DNA Repair helicase Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nucleic Acid Conformation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Thermus thermophilus - enzymology Thermus thermophilus - genetics UvrB |
| title | Structural Insights into the Cryptic DNA-dependent ATPase Activity of UvrB |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T16%3A40%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20Insights%20into%20the%20Cryptic%20DNA-dependent%20ATPase%20Activity%20of%20UvrB&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=Eryilmaz,%20Jitka&rft.date=2006-03-17&rft.volume=357&rft.issue=1&rft.spage=62&rft.epage=72&rft.pages=62-72&rft.issn=0022-2836&rft.eissn=1089-8638&rft_id=info:doi/10.1016/j.jmb.2005.12.059&rft_dat=%3Cproquest_cross%3E17110937%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17110937&rft_id=info:pmid/16426634&rft_els_id=S0022283605016359&rfr_iscdi=true |