| http://purl.uniprot.org/citations/1411536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1411536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1411536 | http://www.w3.org/2000/01/rdf-schema#comment | "The crystal structure of the DNA repair enzyme endonuclease III, which recognizes and cleaves DNA at damaged bases, has been solved to 2.0 angstrom resolution with an R factor of 0.185. This iron-sulfur [4Fe-4S] enzyme is elongated and bilobal with a deep cleft separating two similarly sized domains: a novel, sequence-continuous, six-helix domain (residues 22 to 132) and a Greek-key, four-helix domain formed by the amino-terminal and three carboxyl-terminal helices (residues 1 to 21 and 133 to 211) together with the [4Fe-4S] cluster. The cluster is bound entirely within the carboxyl-terminal loop with a ligation pattern (Cys-X6-Cys-X2-Cys-X5-Cys) distinct from all other known [4Fe-4S] proteins. Sequence conservation and the positive electrostatic potential of conserved regions identify a surface suitable for binding duplex B-DNA across the long axis of the enzyme, matching a 46 angstrom length of protected DNA. The primary role of the [4Fe-4S] cluster appears to involve positioning conserved basic residues for interaction with the DNA phosphate backbone. The crystallographically identified inhibitor binding region, which recognizes the damaged base thymine glycol, is a seven-residue beta-hairpin (residues 113 to 119). Location and side chain orientation at the base of the inhibitor binding site implicate Glu112 in the N-glycosylase mechanism and Lys120 in the beta-elimination mechanism. Overall, the structure reveals an unusual fold and a new biological function for [4Fe-4S] clusters and provides a structural basis for studying recognition of damaged DNA and the N-glycosylase and apurinic/apyrimidinic-lyase mechanisms."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1411536"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1411536"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Tainer J.A."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Tainer J.A."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Cunningham R.P."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Cunningham R.P."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "O'Handley S.F."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "O'Handley S.F."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Fisher C.L."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Fisher C.L."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Kuo C.-F."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "Kuo C.-F."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "McRee D."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/author | "McRee D."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/pages | "434-440"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/pages | "434-440"xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/title | "Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III."xsd:string |
| http://purl.uniprot.org/citations/1411536 | http://purl.uniprot.org/core/title | "Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III."xsd:string |