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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 2575 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 2565 | - |
dc.citation.title | CELL REPORTS | - |
dc.citation.volume | 13 | - |
dc.contributor.author | Liu, Yijin | - |
dc.contributor.author | Freeman, Alasdair D. J. | - |
dc.contributor.author | Declais, Anne-Cecile | - |
dc.contributor.author | Wilson, Timothy J. | - |
dc.contributor.author | Gartner, Anton | - |
dc.contributor.author | Lilley, David M. J. | - |
dc.date.accessioned | 2023-12-22T00:16:38Z | - |
dc.date.available | 2023-12-22T00:16:38Z | - |
dc.date.created | 2020-01-30 | - |
dc.date.issued | 2015-12 | - |
dc.description.abstract | We present the crystal structure of the junction-resolving enzyme GEN1 bound to DNA at 2.5 angstrom resolution. The structure of the GEN1 protein reveals it to have an elaborated FEN-XPG family fold that is modified for its role in four-way junction resolution. The functional unit in the crystal is a monomer of active GEN1 bound to the product of resolution cleavage, with an extensive DNA binding interface for both helical arms. Within the crystal lattice, a GEN1 dimer interface juxtaposes two products, whereby they can be reconnected into a four-way junction, the structure of which agrees with that determined in solution. The reconnection requires some opening of the DNA structure at the center, in agreement with permanganate probing and 2-aminopurine fluorescence. The structure shows that a relaxation of the DNA structure accompanies cleavage, suggesting how second-strand cleavage is accelerated to ensure productive resolution of the junction. | - |
dc.identifier.bibliographicCitation | CELL REPORTS, v.13, no.11, pp.2565 - 2575 | - |
dc.identifier.doi | 10.1016/j.celrep.2015.11.042 | - |
dc.identifier.issn | 2211-1247 | - |
dc.identifier.scopusid | 2-s2.0-84952877095 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/30972 | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S2211124715013571?via%3Dihub | - |
dc.identifier.wosid | 000367101400024 | - |
dc.language | 영어 | - |
dc.publisher | CELL PRESS | - |
dc.title | Crystal Structure of a Eukaryotic GEN1 Resolving Enzyme Bound to DNA | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | HOLLIDAY JUNCTION RESOLVASE | - |
dc.subject.keywordPlus | ENDONUCLEASE | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | CCE1 | - |
dc.subject.keywordPlus | NUCLEASES | - |
dc.subject.keywordPlus | REPAIR | - |
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