3h4d: Difference between revisions

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[[Image:3h4d.jpg|left|200px]]


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==Ternary complex of human DNA polymerase iota with template U/T and incoming dGTP==
The line below this paragraph, containing "STRUCTURE_3h4d", creates the "Structure Box" on the page.
<StructureSection load='3h4d' size='340' side='right'caption='[[3h4d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3h4d]] is a 3 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=3H4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4D FirstGlance]. <br>
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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]] 2.2&#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=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_3h4d|  PDB=3h4d  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4d OCA], [https://pdbe.org/3h4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h4d RCSB], [https://www.ebi.ac.uk/pdbsum/3h4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POLI_HUMAN POLI_HUMAN] Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.<ref>PMID:11013228</ref> <ref>PMID:11251121</ref> <ref>PMID:11387224</ref> <ref>PMID:12410315</ref> <ref>PMID:14630940</ref> <ref>PMID:15199127</ref> <ref>PMID:15254543</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/3h4d_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=3h4d ConSurf].
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== Publication Abstract from PubMed ==
Human DNA polymerase-iota (Poliota) incorporates correct nucleotides opposite template purines with a much higher efficiency and fidelity than opposite template pyrimidines. In fact, the fidelity opposite template T is so poor that Poliota inserts an incorrect dGTP approximately 10 times better than it inserts the correct dATP. We determine here how a template T/U is accommodated in the Poliota active site and why a G is incorporated more efficiently than an A. We show that in the absence of incoming dATP or dGTP (binary complex), template T/U exists in both syn and anti conformations, but in the presence of dATP or dGTP (ternary complexes), template T/U is predominantly in the anti conformation. We also show that dATP and dGTP insert differently opposite template T/U, and that the basis of selection of dGTP over dATP is a hydrogen bond between the N2 amino group of dGTP and Gln59 of Poliota.


===Ternary complex of human DNA polymerase iota with template U/T and incoming dGTP===
Replication across template T/U by human DNA polymerase-iota.,Jain R, Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK Structure. 2009 Jul 15;17(7):974-80. PMID:19604477<ref>PMID:19604477</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3h4d" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
3H4D is a 3 chains structure of sequences 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=3H4D OCA].
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
[[Category: DNA-directed DNA polymerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Aggarwal, A K.]]
[[Category: Large Structures]]
[[Category: Jain, R.]]
[[Category: Aggarwal AK]]
[[Category: Johnson, R E.]]
[[Category: Jain R]]
[[Category: Nair, D T.]]
[[Category: Johnson RE]]
[[Category: Prakash, L.]]
[[Category: Nair DT]]
[[Category: Prakash, S.]]
[[Category: Prakash L]]
[[Category: Dna damage]]
[[Category: Prakash S]]
[[Category: Dna polymerase iota]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Dna synthesis]]
[[Category: Dna-binding]]
[[Category: Dna-directed dna polymerase]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Mutator protein]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleus]]
[[Category: Polymorphism]]
[[Category: Replication]]
[[Category: Replication/dna complex]]
[[Category: Schiff base]]
[[Category: Transferase]]
 
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