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dc.contributor.author황광연-
dc.contributor.author백규원-
dc.contributor.author김혜연-
dc.contributor.author조윤제-
dc.date.accessioned2015-12-02T05:41:08Z-
dc.date.available2015-12-02T05:41:08Z-
dc.date.issued199808-
dc.identifier.citationVOL 5, NO 8, 707-713-
dc.identifier.issn1072-8368-
dc.identifier.other9608-
dc.identifier.urihttp://pubs.kist.re.kr/handle/201004/18668-
dc.description.abstractFlap endonuclease-1 (FEN-1), a structure specific nuclease, is an essential enzyme for eukaryotic DNA replication and repair. The crystal structure of FEN-1 from Methanococcus jannaschii, determined at 2.0 Å resolution, reveals an active site with two metal ions residing on top of a deep cleft where several conserved acidic residues are clustered. Near the active site, a long flexible loop comprised of many basic and aromatic residues forms a hole large enough to accommodate the DNA substrate. Deletion mutations in this loop significantly decreased the nuclease activity and specificity of FEN-1, suggesting that the loop is critical for recognition and cleavage of the junction between single and double-stranded regions of flap DNA.-
dc.publisherNature structural biology-
dc.titleThe crystal structure of flap endonuclease-1 from methanococcus jannaschii-
dc.typeArticle-
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