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[[Image:1kdh.jpg|left|200px]]


{{Structure
==Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA==
|PDB= 1kdh |SIZE=350|CAPTION= <scene name='initialview01'>1kdh</scene>, resolution 3.00&Aring;
<StructureSection load='1kdh' size='340' side='right'caption='[[1kdh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
<table><tr><td colspan='2'>[[1kdh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDH FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_nucleotidylexotransferase DNA nucleotidylexotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.31 2.7.7.31]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1kdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdh OCA], [https://pdbe.org/1kdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdh RCSB], [https://www.ebi.ac.uk/pdbsum/1kdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TDT_MOUSE TDT_MOUSE] Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
== 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/kd/1kdh_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=1kdh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the catalytic core of murine terminal deoxynucleotidyltransferase (TdT) at 2.35 A resolution reveals a typical DNA polymerase beta-like fold locked in a closed form. In addition, the structures of two different binary complexes, one with an oligonucleotide primer and the other with an incoming ddATP-Co(2+) complex, show that the substrates and the two divalent ions in the catalytic site are positioned in TdT in a manner similar to that described for the human DNA polymerase beta ternary complex, suggesting a common two metal ions mechanism of nucleotidyl transfer in these two proteins. The inability of TdT to accommodate a template strand can be explained by steric hindrance at the catalytic site caused by a long lariat-like loop, which is absent in DNA polymerase beta. However, displacement of this discriminating loop would be sufficient to unmask a number of evolutionarily conserved residues, which could then interact with a template DNA strand. The present structure can be used to model the recently discovered human polymerase mu, with which it shares 43% sequence identity.


'''Binary Complex of Murine Terminal Deoxynucleotidyl Transferase with a Primer Single Stranded DNA'''
Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase.,Delarue M, Boule JB, Lescar J, Expert-Bezancon N, Jourdan N, Sukumar N, Rougeon F, Papanicolaou C EMBO J. 2002 Feb 1;21(3):427-39. PMID:11823435<ref>PMID:11823435</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kdh" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The crystal structure of the catalytic core of murine terminal deoxynucleotidyltransferase (TdT) at 2.35 A resolution reveals a typical DNA polymerase beta-like fold locked in a closed form. In addition, the structures of two different binary complexes, one with an oligonucleotide primer and the other with an incoming ddATP-Co(2+) complex, show that the substrates and the two divalent ions in the catalytic site are positioned in TdT in a manner similar to that described for the human DNA polymerase beta ternary complex, suggesting a common two metal ions mechanism of nucleotidyl transfer in these two proteins. The inability of TdT to accommodate a template strand can be explained by steric hindrance at the catalytic site caused by a long lariat-like loop, which is absent in DNA polymerase beta. However, displacement of this discriminating loop would be sufficient to unmask a number of evolutionarily conserved residues, which could then interact with a template DNA strand. The present structure can be used to model the recently discovered human polymerase mu, with which it shares 43% sequence identity.
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1KDH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDH OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase., Delarue M, Boule JB, Lescar J, Expert-Bezancon N, Jourdan N, Sukumar N, Rougeon F, Papanicolaou C, EMBO J. 2002 Feb 1;21(3):427-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11823435 11823435]
[[Category: DNA nucleotidylexotransferase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Boule JB]]
[[Category: Boule, J B.]]
[[Category: Delarue M]]
[[Category: Delarue, M.]]
[[Category: Expert-Bezancon N]]
[[Category: Expert-Bezancon, N.]]
[[Category: Jourdan N]]
[[Category: Jourdan, N.]]
[[Category: Lescar J]]
[[Category: Lescar, J.]]
[[Category: Papanicolaou C]]
[[Category: Papanicolaou, C.]]
[[Category: Rougeon F]]
[[Category: Rougeon, F.]]
[[Category: Sukumar N]]
[[Category: Sukumar, N.]]
[[Category: MG]]
[[Category: NA]]
[[Category: nucleotidyl transferase]]
[[Category: polymerase]]
 
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Retrieved from "https://proteopedia.org/1kdh"