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dc.contributor.authorKuo, C.en_US
dc.contributor.authorMcRee, D.en_US
dc.contributor.authorFisher, C.en_US
dc.contributor.authorO'Handley, Suzanneen_US
dc.contributor.authorCunningham, R.en_US
dc.contributor.authorTainer, J.en_US
dc.date.accessioned2006-07-19T19:49:28Zen_US
dc.date.available2006-07-19T19:49:28Zen_US
dc.date.issued1992-10-16en_US
dc.identifier.citationScience 258N5081 (1992) 434-440en_US
dc.identifier.issn1095-9203en_US
dc.identifier.urihttp://hdl.handle.net/1850/2196en_US
dc.description.abstractThe 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.en_US
dc.format.extent26767 bytesen_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoen_USen_US
dc.publisherAmerican Association for the Advancement of Science: Scienceen_US
dc.subjectAtomic structureen_US
dc.subjectDNAen_US
dc.subjectEnzymesen_US
dc.titleAtomic structure of the DNA repair [4Fe-4S] enzyme endonuclease IIIen_US
dc.typeAbstracten_US
dc.identifier.urlhttp://dx.doi.org/10.1126/science.1411536


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