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| [[Image:2okv.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2okv| PDB=2okv | SCENE= }} | | {{STRUCTURE_2okv| PDB=2okv | SCENE= }} |
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| '''c-Myc DNA Unwinding Element Binding Protein'''
| | ===c-Myc DNA Unwinding Element Binding Protein=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17264083}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17264083 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17264083}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Due]] | | [[Category: Due]] |
| [[Category: Trna deacylase]] | | [[Category: Trna deacylase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:07:19 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:09:15 2008'' |
