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http://purl.uniprot.org/citations/17264083http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17264083http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17264083http://www.w3.org/2000/01/rdf-schema#comment"Local zones of easily unwound DNA are characteristic of prokaryotic and eukaryotic replication origins. The DNA-unwinding element of the human c-myc replication origin is essential for replicator activity and is a target of the DNA-unwinding element-binding protein DUE-B in vivo. We present here the 2.0A crystal structure of DUE-B and complementary biochemical characterization of its biological activity. The structure corresponds to a dimer of the N-terminal domain of the full-length protein and contains many of the structural elements of the nucleotide binding fold. A single magnesium ion resides in the putative active site cavity, which could serve to facilitate ATP hydrolytic activity of this protein. The structure also demonstrates a notable similarity to those of tRNA-editing enzymes. Consistent with this structural homology, the N-terminal core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity. We further demonstrate that the C-terminal portion of the enzyme is disordered and not essential for dimerization. However, this region is essential for DNA binding in vitro and becomes ordered in the presence of DNA."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609632200"xsd:string
http://purl.uniprot.org/citations/17264083http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609632200"xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Nair S.K."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Nair S.K."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Ghosh M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Ghosh M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Yu J.P."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Yu J.P."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Bae B."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Bae B."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Kemp M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Kemp M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Leffak M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/author"Leffak M."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/pages"10441-10448"xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/pages"10441-10448"xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/title"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B."xsd:string
http://purl.uniprot.org/citations/17264083http://purl.uniprot.org/core/title"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B."xsd:string