2okv: Difference between revisions

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[[Image:2okv.png|left|200px]]


{{STRUCTURE_2okv| PDB=2okv | SCENE= }}
==c-Myc DNA Unwinding Element Binding Protein==
<StructureSection load='2okv' size='340' side='right'caption='[[2okv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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'>[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>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/2okv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===c-Myc DNA Unwinding Element Binding Protein===
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>


{{ABSTRACT_PUBMED_17264083}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2okv" style="background-color:#fffaf0;"></div>
[[2okv]] is a 4 chain structure with 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].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:017264083</ref><references group="xtra"/>
</StructureSection>
[[Category: Homo sapiens]]
[[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]]
Retrieved from "https://proteopedia.org/2okv"