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| | ==c-Myc DNA Unwinding Element Binding Protein== | | ==c-Myc DNA Unwinding Element Binding Protein== |
| - | <StructureSection load='2okv' size='340' side='right' caption='[[2okv]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2okv' size='340' side='right'caption='[[2okv]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2okv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OKV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2okv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OKV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HARS2, C20orf88 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2okv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okv OCA], [http://pdbe.org/2okv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2okv RCSB], [http://www.ebi.ac.uk/pdbsum/2okv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2okv ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2okv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okv OCA], [https://pdbe.org/2okv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2okv RCSB], [https://www.ebi.ac.uk/pdbsum/2okv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2okv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DTD1_HUMAN DTD1_HUMAN]] Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (Potential). | + | [https://www.uniprot.org/uniprot/DTD1_HUMAN DTD1_HUMAN] Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (Potential). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Bae, B]] | + | [[Category: Large Structures]] |
| - | [[Category: Nair, S K]] | + | [[Category: Bae B]] |
| - | [[Category: Atpase]] | + | [[Category: Nair SK]] |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Due]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Trna deacylase]]
| + | |
| Structural highlights
Function
DTD1_HUMAN Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (Potential).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B.,Kemp M, Bae B, Yu JP, Ghosh M, Leffak M, Nair SK J Biol Chem. 2007 Apr 6;282(14):10441-8. Epub 2007 Jan 30. PMID:17264083[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kemp M, Bae B, Yu JP, Ghosh M, Leffak M, Nair SK. Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B. J Biol Chem. 2007 Apr 6;282(14):10441-8. Epub 2007 Jan 30. PMID:17264083 doi:10.1074/jbc.M609632200
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