Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core
Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr$^{342}$ is attached to the 3′-phosphate of the...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1997-04, Vol.276 (5309), p.126-131 |
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| creator | Kwon, Hyock Joo Tirumalai, Radhakrishna Landy, Arthur Ellenberger, Tom |
| description | Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr$^{342}$ is attached to the 3′-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr$^{342}$ nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA. |
| doi_str_mv | 10.1126/science.276.5309.126 |
| format | Article |
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DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr$^{342}$ is attached to the 3′-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr$^{342}$ nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.276.5309.126</identifier><identifier>PMID: 9082984</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Active sites ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Attachment Sites, Microbiological ; Bacteriophage lambda - enzymology ; Bacteriophages ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Cloning, Molecular ; Conserved Sequence ; Crystal structure ; Crystallography, X-Ray ; Crystals ; Deoxyribonucleic acid ; DNA ; DNA - metabolism ; DNA cleavage ; DNA Nucleotidyltransferases - chemistry ; DNA Nucleotidyltransferases - metabolism ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Genetic recombination ; Hydrogen Bonding ; Hydrolases ; Integrases - chemistry ; Integrases - metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleophiles ; phage lambda ; Phosphates ; Physiological aspects ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein subunits ; Proteins ; Recombinant DNA ; Recombinases ; Recombination, Genetic ; Tyrosine - chemistry ; Tyrosine - metabolism ; Virus Integration</subject><ispartof>Science (American Association for the Advancement of Science), 1997-04, Vol.276 (5309), p.126-131</ispartof><rights>Copyright 1997 American Association for the Advancement of Science</rights><rights>1997 INIST-CNRS</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 4, 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c883t-e216be94f1329226a2ba101c342b5d7f8bec9f49a516566aa6f52f1f572405253</citedby><cites>FETCH-LOGICAL-c883t-e216be94f1329226a2ba101c342b5d7f8bec9f49a516566aa6f52f1f572405253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2892615$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2892615$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2627014$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9082984$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kwon, Hyock Joo</creatorcontrib><creatorcontrib>Tirumalai, Radhakrishna</creatorcontrib><creatorcontrib>Landy, Arthur</creatorcontrib><creatorcontrib>Ellenberger, Tom</creatorcontrib><title>Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr$^{342}$ is attached to the 3′-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr$^{342}$ nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.</description><subject>Active sites</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Attachment Sites, Microbiological</subject><subject>Bacteriophage lambda - enzymology</subject><subject>Bacteriophages</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Conserved Sequence</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA cleavage</subject><subject>DNA Nucleotidyltransferases - chemistry</subject><subject>DNA Nucleotidyltransferases - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic recombination</subject><subject>Hydrogen Bonding</subject><subject>Hydrolases</subject><subject>Integrases - chemistry</subject><subject>Integrases - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleophiles</subject><subject>phage lambda</subject><subject>Phosphates</subject><subject>Physiological aspects</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein subunits</subject><subject>Proteins</subject><subject>Recombinant DNA</subject><subject>Recombinases</subject><subject>Recombination, Genetic</subject><subject>Tyrosine - chemistry</subject><subject>Tyrosine - metabolism</subject><subject>Virus Integration</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN019rUzEUAPCLKLNOv8GEiwz1Ya35c5Ob-CDM6mqhrLCpryE3PbdLuU1mkivrtzejZVoZOvIQOOeXAzmcUxRHGI0wJvxdNBacgRGp-YhRJEc5-KgYYCTZUBJEHxcDhCgfClSzp8WzGFcI5ZykB8WBRIJIUQ2Ki7MObmxjO5s2pXXlp_PT8gKMXzfW6WS9e19eptCb1AcofVumKyhnet0sdDl1CZZBRyjHOuluk6wpxz7A8-JJq7sIL3b3YfHt7PPX8ZfhbD6Zjk9nQyMETUMgmDcgqxZTIgnhmjQaI2xoRRq2qFvRgJFtJTXDnHGuNW8ZaXHLalIhRhg9LD5s6173zRoWBlwKulPXwa512CivrdrPOHullv6nwoJKQapc4PWuQPA_eohJrW000HXage-jqoXIPcoNOyze_BtWlNeY8v-XxEzwqhYkw1d_wZXvg8v9UgRTVjNc1RmdbNFSd6Csa33-h1mCg_wd76C1OXyKJcVCIJr58B6ezwLW1tzn3-75TBLcpKXuY1TTy_MH0_n3B9OPk4dSMZnt0ZP7qPFdB0tQebDG8z1ebbkJPsYA7d1YYKRut0fttkfl7VG326NyMD97-edI3T3arUvOH-_yOhrdtUE7Y-MdI5zUCN-yoy1bxeTD77SQhGNGfwGvJyeM</recordid><startdate>19970404</startdate><enddate>19970404</enddate><creator>Kwon, Hyock Joo</creator><creator>Tirumalai, Radhakrishna</creator><creator>Landy, Arthur</creator><creator>Ellenberger, Tom</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>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><scope>5PM</scope></search><sort><creationdate>19970404</creationdate><title>Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core</title><author>Kwon, Hyock Joo ; Tirumalai, Radhakrishna ; Landy, Arthur ; Ellenberger, Tom</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c883t-e216be94f1329226a2ba101c342b5d7f8bec9f49a516566aa6f52f1f572405253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Active sites</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Attachment Sites, Microbiological</topic><topic>Bacteriophage lambda - enzymology</topic><topic>Bacteriophages</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Conserved Sequence</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Crystals</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA - metabolism</topic><topic>DNA cleavage</topic><topic>DNA Nucleotidyltransferases - chemistry</topic><topic>DNA Nucleotidyltransferases - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic recombination</topic><topic>Hydrogen Bonding</topic><topic>Hydrolases</topic><topic>Integrases - chemistry</topic><topic>Integrases - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nucleophiles</topic><topic>phage lambda</topic><topic>Phosphates</topic><topic>Physiological aspects</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein subunits</topic><topic>Proteins</topic><topic>Recombinant DNA</topic><topic>Recombinases</topic><topic>Recombination, Genetic</topic><topic>Tyrosine - chemistry</topic><topic>Tyrosine - metabolism</topic><topic>Virus Integration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwon, Hyock Joo</creatorcontrib><creatorcontrib>Tirumalai, Radhakrishna</creatorcontrib><creatorcontrib>Landy, Arthur</creatorcontrib><creatorcontrib>Ellenberger, 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Tom</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1997-04-04</date><risdate>1997</risdate><volume>276</volume><issue>5309</issue><spage>126</spage><epage>131</epage><pages>126-131</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr$^{342}$ is attached to the 3′-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr$^{342}$ nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9082984</pmid><doi>10.1126/science.276.5309.126</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1997-04, Vol.276 (5309), p.126-131 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1839824 |
| source | MEDLINE; American Association for the Advancement of Science; JSTOR |
| subjects | Active sites Amino Acid Sequence Analytical, structural and metabolic biochemistry Attachment Sites, Microbiological Bacteriophage lambda - enzymology Bacteriophages Binding Sites Biochemistry Biological and medical sciences Cloning, Molecular Conserved Sequence Crystal structure Crystallography, X-Ray Crystals Deoxyribonucleic acid DNA DNA - metabolism DNA cleavage DNA Nucleotidyltransferases - chemistry DNA Nucleotidyltransferases - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Genetic recombination Hydrogen Bonding Hydrolases Integrases - chemistry Integrases - metabolism Models, Molecular Molecular Sequence Data Nucleophiles phage lambda Phosphates Physiological aspects Protein Conformation Protein Folding Protein Structure, Secondary Protein subunits Proteins Recombinant DNA Recombinases Recombination, Genetic Tyrosine - chemistry Tyrosine - metabolism Virus Integration |
| title | Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core |
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