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[[Image:5ktq.gif|left|200px]]


{{Structure
==LARGE FRAGMENT OF TAQ DNA POLYMERASE BOUND TO DCTP==
|PDB= 5ktq |SIZE=350|CAPTION= <scene name='initialview01'>5ktq</scene>, resolution 2.50&Aring;
<StructureSection load='5ktq' size='340' side='right'caption='[[5ktq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=DCP:2&#39;-DEOXYCYTIDINE-5&#39;-TRIPHOSPHATE'>DCP</scene>
<table><tr><td colspan='2'>[[5ktq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTQ FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= TAQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</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=5ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktq OCA], [https://pdbe.org/5ktq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ktq RCSB], [https://www.ebi.ac.uk/pdbsum/5ktq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPO1_THEAQ DPO1_THEAQ]  
== 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/kt/5ktq_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=5ktq ConSurf].
<div style="clear:both"></div>


'''LARGE FRAGMENT OF TAQ DNA POLYMERASE BOUND TO DCTP'''
==See Also==
 
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structures of the Klenow fragment of the Thermus aquaticus DNA polymerase I (Klentaq1) complexed with four deoxyribonucleoside triphosphates (dNTP) have been determined to 2.5 A resolution. The dNTPs bind adjacent to the O helix of Klentaq1. The triphosphate moieties are at nearly identical positions in all four complexes and are anchored by three positively charged residues, Arg659, Lys663, and Arg587, and by two polar residues, His639 and Gln613. The configuration of the base moieties in the Klentaq1/dNTP complexes demonstrates variability suggesting that dNTP binding is primarily determined by recognition and binding of the phosphate moiety. However, when superimposed on the Taq polymerase/blunt end DNA complex structure (Eom et al., 1996), two of the dNTP/Klentaq1 structures demonstrate appropriate stacking of the nucleotide base with the 3' end of the DNA primer strand, suggesting that at least in these two binary complexes, the observed dNTP conformations are functionally relevant.
[[Category: Large Structures]]
 
==About this Structure==
5KTQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTQ OCA].
 
==Reference==
Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates., Li Y, Kong Y, Korolev S, Waksman G, Protein Sci. 1998 May;7(5):1116-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9605316 9605316]
[[Category: DNA-directed DNA polymerase]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Kong, Y.]]
[[Category: Kong Y]]
[[Category: Korolev, S.]]
[[Category: Korolev S]]
[[Category: Li, Y.]]
[[Category: Li Y]]
[[Category: Waksman, G.]]
[[Category: Waksman G]]
[[Category: DCP]]
[[Category: large fragement of taq dna polymerase i]]
 
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