Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69
The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except r...
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| Veröffentlicht in: | Cell 1997-06, Vol.89 (7), p.1087-1099 |
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| container_title | Cell |
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| creator | Wang, J Sattar, A K Wang, C C Karam, J D Konigsberg, W H Steitz, T A |
| description | The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases. |
| doi_str_mv | 10.1016/S0092-8674(00)80296-2 |
| format | Article |
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Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases.</description><identifier>ISSN: 0092-8674</identifier><identifier>DOI: 10.1016/S0092-8674(00)80296-2</identifier><identifier>PMID: 9215631</identifier><language>eng</language><publisher>United States</publisher><subject>AIDS/HIV ; Bacteriophages - chemistry ; Bacteriophages - enzymology ; Bacteriophages - genetics ; Binding Sites - physiology ; Conserved Sequence ; Crystallography ; DNA Polymerase I - chemistry ; DNA Polymerase I - genetics ; DNA Polymerase II - chemistry ; DNA Polymerase II - genetics ; DNA Polymerase II - metabolism ; DNA, Single-Stranded - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Exonucleases - chemistry ; Exonucleases - metabolism ; Gene Expression Regulation, Viral - physiology ; HIV - chemistry ; HIV - enzymology ; phage RB69 ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Replication Origin - physiology ; RNA-Directed DNA Polymerase - chemistry ; RNA-Directed DNA Polymerase - genetics ; Sequence Homology, Amino Acid</subject><ispartof>Cell, 1997-06, Vol.89 (7), p.1087-1099</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-e153b4cc93f08bac1fb3a796a7d0d771a026a215c8ee5a60c7db5d9bbdcdc57a3</citedby><cites>FETCH-LOGICAL-c434t-e153b4cc93f08bac1fb3a796a7d0d771a026a215c8ee5a60c7db5d9bbdcdc57a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9215631$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, J</creatorcontrib><creatorcontrib>Sattar, A K</creatorcontrib><creatorcontrib>Wang, C C</creatorcontrib><creatorcontrib>Karam, J D</creatorcontrib><creatorcontrib>Konigsberg, W H</creatorcontrib><creatorcontrib>Steitz, T A</creatorcontrib><title>Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69</title><title>Cell</title><addtitle>Cell</addtitle><description>The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases.</description><subject>AIDS/HIV</subject><subject>Bacteriophages - chemistry</subject><subject>Bacteriophages - enzymology</subject><subject>Bacteriophages - genetics</subject><subject>Binding Sites - physiology</subject><subject>Conserved Sequence</subject><subject>Crystallography</subject><subject>DNA Polymerase I - chemistry</subject><subject>DNA Polymerase I - genetics</subject><subject>DNA Polymerase II - chemistry</subject><subject>DNA Polymerase II - genetics</subject><subject>DNA Polymerase II - metabolism</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Exonucleases - chemistry</subject><subject>Exonucleases - metabolism</subject><subject>Gene Expression Regulation, Viral - physiology</subject><subject>HIV - chemistry</subject><subject>HIV - enzymology</subject><subject>phage RB69</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Replication Origin - physiology</subject><subject>RNA-Directed DNA Polymerase - chemistry</subject><subject>RNA-Directed DNA Polymerase - genetics</subject><subject>Sequence Homology, Amino Acid</subject><issn>0092-8674</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOxDAQRV2AlmXhE1ZyhaAIjOPYjstleUorkHg0NNbEcSAo2QQ7KfL3ZB-ipRppdO6d0SFkzuCSAZNXrwA6jlKpknOAixRiLaP4gEz_1kfkOIRvAEiFEBMy0TETkrMp-Vj6IXRY0dD53na9d7QpKNK2qShW7RfSAuuyGqh3bVVa7MpmTW-eFhtgqJ3H4Gjhm5pmaDvny2aMfDr6ci31CTkssArudD9n5P3u9m35EK2e7x-Xi1VkE550kWOCZ4m1mheQji2syDgqLVHlkCvFEGKJ47s2dU6gBKvyTOQ6y3KbW6GQz8jZrrf1zU_vQmfqMlhXVbh2TR-M0gxSLti_IJOQxFyKERQ70PomBO8K0_qyRj8YBmYj3GyFm41ZA2C2wk085ub7A31Wu_wvtbfNfwGOm36-</recordid><startdate>19970627</startdate><enddate>19970627</enddate><creator>Wang, J</creator><creator>Sattar, A K</creator><creator>Wang, C C</creator><creator>Karam, J D</creator><creator>Konigsberg, W H</creator><creator>Steitz, T A</creator><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><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19970627</creationdate><title>Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69</title><author>Wang, J ; Sattar, A K ; Wang, C C ; Karam, J D ; Konigsberg, W H ; Steitz, T A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-e153b4cc93f08bac1fb3a796a7d0d771a026a215c8ee5a60c7db5d9bbdcdc57a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>AIDS/HIV</topic><topic>Bacteriophages - chemistry</topic><topic>Bacteriophages - enzymology</topic><topic>Bacteriophages - genetics</topic><topic>Binding Sites - physiology</topic><topic>Conserved Sequence</topic><topic>Crystallography</topic><topic>DNA Polymerase I - chemistry</topic><topic>DNA Polymerase I - genetics</topic><topic>DNA Polymerase II - chemistry</topic><topic>DNA Polymerase II - genetics</topic><topic>DNA Polymerase II - metabolism</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Exonucleases - chemistry</topic><topic>Exonucleases - metabolism</topic><topic>Gene Expression Regulation, Viral - physiology</topic><topic>HIV - chemistry</topic><topic>HIV - enzymology</topic><topic>phage RB69</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Replication Origin - physiology</topic><topic>RNA-Directed DNA Polymerase - chemistry</topic><topic>RNA-Directed DNA Polymerase - genetics</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, J</creatorcontrib><creatorcontrib>Sattar, A K</creatorcontrib><creatorcontrib>Wang, C C</creatorcontrib><creatorcontrib>Karam, J D</creatorcontrib><creatorcontrib>Konigsberg, W H</creatorcontrib><creatorcontrib>Steitz, T A</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><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, J</au><au>Sattar, A K</au><au>Wang, C C</au><au>Karam, J D</au><au>Konigsberg, W H</au><au>Steitz, T A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1997-06-27</date><risdate>1997</risdate><volume>89</volume><issue>7</issue><spage>1087</spage><epage>1099</epage><pages>1087-1099</pages><issn>0092-8674</issn><abstract>The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases.</abstract><cop>United States</cop><pmid>9215631</pmid><doi>10.1016/S0092-8674(00)80296-2</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Open Access: Cell Press Free Archives; Elsevier ScienceDirect Journals; EZB Electronic Journals Library |
| subjects | AIDS/HIV Bacteriophages - chemistry Bacteriophages - enzymology Bacteriophages - genetics Binding Sites - physiology Conserved Sequence Crystallography DNA Polymerase I - chemistry DNA Polymerase I - genetics DNA Polymerase II - chemistry DNA Polymerase II - genetics DNA Polymerase II - metabolism DNA, Single-Stranded - metabolism Escherichia coli Escherichia coli - genetics Exonucleases - chemistry Exonucleases - metabolism Gene Expression Regulation, Viral - physiology HIV - chemistry HIV - enzymology phage RB69 Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Replication Origin - physiology RNA-Directed DNA Polymerase - chemistry RNA-Directed DNA Polymerase - genetics Sequence Homology, Amino Acid |
| title | Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69 |
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