http://purl.uniprot.org/citations/17264083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17264083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17264083 | http://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/17264083 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m609632200"xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m609632200"xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Nair S.K."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Nair S.K."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Ghosh M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Ghosh M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Yu J.P."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Yu J.P."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Bae B."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Bae B."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Kemp M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Kemp M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Leffak M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/author | "Leffak M."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/pages | "10441-10448"xsd:string |
http://purl.uniprot.org/citations/17264083 | http://purl.uniprot.org/core/pages | "10441-10448"xsd:string |
http://purl.uniprot.org/citations/17264083 | http://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/17264083 | http://purl.uniprot.org/core/title | "Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B."xsd:string |