Atomic Structure of the Clamp Loader Small Subunit from Pyrococcus furiosus
In eukaryotic DNA replication, replication factor-C (RFC) acts as the clamp loader, which correctly installs the sliding clamp onto DNA strands at replication forks. The eukaryotic RFC is a complex consisting of one large and four small subunits. We have determined the crystal structure of the clamp...
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| Veröffentlicht in: | Molecular cell 2001-08, Vol.8 (2), p.455-463 |
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| creator | Oyama, Takuji Ishino, Yoshizumi Cann, Isaac K.O. Ishino, Sonoko Morikawa, Kosuke |
| description | In eukaryotic DNA replication, replication factor-C (RFC) acts as the clamp loader, which correctly installs the sliding clamp onto DNA strands at replication forks. The eukaryotic RFC is a complex consisting of one large and four small subunits. We have determined the crystal structure of the clamp loader small subunit (RFCS) from
Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers. The crescent-like architecture of each subunit formed by the three domains resembles that of the δ′ subunit of the
E. coli clamp loader. The trimeric architecture of archaeal RFCS, with its mobile N-terminal domains, involves intersubunit interactions that may be conserved in eukaryotic functional complexes. |
| doi_str_mv | 10.1016/S1097-2765(01)00328-8 |
| format | Article |
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Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers. The crescent-like architecture of each subunit formed by the three domains resembles that of the δ′ subunit of the
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Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers. The crescent-like architecture of each subunit formed by the three domains resembles that of the δ′ subunit of the
E. coli clamp loader. The trimeric architecture of archaeal RFCS, with its mobile N-terminal domains, involves intersubunit interactions that may be conserved in eukaryotic functional complexes.</description><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>DNA Replication - physiology</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Subunits</subject><subject>Proteins - chemistry</subject><subject>Pyrococcus furiosus</subject><subject>Pyrococcus furiosus - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Replication Protein C</subject><subject>Sequence Alignment</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMofv8EJSfRQzXTNk16kmXxCxcUVs-hO5lipN2sSSP4790v8OhphuGZd4aHsTMQ1yCgupmCqFWWq0peCrgSosh1pnfY4XpcQlXubvsVcsCOYvwUAkqp6312ACBLqUp1yJ5Hg-8d8ukQEg4pEPctHz6Ij7umX_CJbywFPu2bruPTNEtzN_A2-J6__gSPHjFF3qbgfEzxhO21TRfpdFuP2fv93dv4MZu8PDyNR5MMpZBDVteEWpCUSluUeSVrxJkF2dZtVRZgCxSqqOqqJIuoKW_ICqGkyotaCih0ccwuNrmL4L8SxcH0LiJ1XTMnn6JRAFpWRfkvCBqWwVItQbkBMfgYA7VmEVzfhB8Dwqx0m7Vus3JpBJi1brP65Hx7IM16sn9bW79L4HYD0NLHt6NgIjqaI1kXCAdjvfvnxC-A245V</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Oyama, Takuji</creator><creator>Ishino, Yoshizumi</creator><creator>Cann, Isaac K.O.</creator><creator>Ishino, Sonoko</creator><creator>Morikawa, Kosuke</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20010801</creationdate><title>Atomic Structure of the Clamp Loader Small Subunit from Pyrococcus furiosus</title><author>Oyama, Takuji ; 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The eukaryotic RFC is a complex consisting of one large and four small subunits. We have determined the crystal structure of the clamp loader small subunit (RFCS) from
Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers. The crescent-like architecture of each subunit formed by the three domains resembles that of the δ′ subunit of the
E. coli clamp loader. The trimeric architecture of archaeal RFCS, with its mobile N-terminal domains, involves intersubunit interactions that may be conserved in eukaryotic functional complexes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11545747</pmid><doi>10.1016/S1097-2765(01)00328-8</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Archaeal Proteins - chemistry Bacterial Proteins - chemistry Binding Sites Crystallography, X-Ray Dimerization DNA Replication - physiology DNA-Binding Proteins - chemistry Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Quaternary Protein Subunits Proteins - chemistry Pyrococcus furiosus Pyrococcus furiosus - chemistry Recombinant Proteins - chemistry Recombinant Proteins - genetics Replication Protein C Sequence Alignment |
| title | Atomic Structure of the Clamp Loader Small Subunit from Pyrococcus furiosus |
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