2okv

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{{Seed}}
 
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[[Image:2okv.png|left|200px]]
 
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==c-Myc DNA Unwinding Element Binding Protein==
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The line below this paragraph, containing "STRUCTURE_2okv", creates the "Structure Box" on the page.
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<StructureSection load='2okv' size='340' side='right'caption='[[2okv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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>
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{{STRUCTURE_2okv| PDB=2okv | SCENE= }}
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<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>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/2okv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2okv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===c-Myc DNA Unwinding Element Binding Protein===
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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<ref>PMID:17264083</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17264083}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2okv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17264083 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17264083}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2OKV is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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;282(14):10441-8. Epub 2007 Jan 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17264083 17264083]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bae, B.]]
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[[Category: Bae B]]
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[[Category: Nair, S K.]]
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[[Category: Nair SK]]
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[[Category: Atpase]]
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[[Category: Dna replication]]
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[[Category: Due]]
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[[Category: Trna deacylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:09:15 2008''
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Current revision

c-Myc DNA Unwinding Element Binding Protein

PDB ID 2okv

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OCA

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