2aq4

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(New page: 200px<br /><applet load="2aq4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aq4, resolution 2.32&Aring;" /> '''Ternary complex of t...)
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[[Image:2aq4.gif|left|200px]]<br /><applet load="2aq4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2aq4, resolution 2.32&Aring;" />
 
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'''Ternary complex of the catalytic core of REV1 with DNA and dCTP.'''<br />
 
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==Overview==
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==Ternary complex of the catalytic core of REV1 with DNA and dCTP.==
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The Rev1 DNA polymerase is highly specialized for the incorporation of C, opposite template G. We present here the crystal structure of yeast Rev1, bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates the identity of the, incoming nucleotide, as well as the identity of the templating base., Template G and incoming dCTP do not pair with each other. Instead, the, template G is evicted from the DNA helix, and it makes optimal hydrogen, bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming, dCTP pairs with an arginine rather than the templating base, which ensures, the incorporation of dCTP over other incoming nucleotides. This mechanism, provides an elegant means for promoting proficient and error-free, synthesis through N2-adducted guanines that obstruct replication.
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<StructureSection load='2aq4' size='340' side='right'caption='[[2aq4]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2aq4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AQ4 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]] 2.32&#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=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=2aq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aq4 OCA], [https://pdbe.org/2aq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aq4 RCSB], [https://www.ebi.ac.uk/pdbsum/2aq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aq4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/REV1_YEAST REV1_YEAST] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.<ref>PMID:8751446</ref> <ref>PMID:11316789</ref> <ref>PMID:16452144</ref>
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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/aq/2aq4_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=2aq4 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2AQ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and DCP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AQ4 OCA].
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Rev1 employs a novel mechanism of DNA synthesis using a protein template., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Science. 2005 Sep 30;309(5744):2219-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16195463 16195463]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Aggarwal AK]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Johnson RE]]
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[[Category: Johnson, R.E.]]
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[[Category: Nair DT]]
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[[Category: Nair, D.T.]]
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[[Category: Prakash L]]
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[[Category: Prakash, L.]]
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[[Category: Prakash S]]
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[[Category: Prakash, S.]]
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[[Category: DCP]]
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[[Category: MG]]
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[[Category: g-loop]]
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[[Category: n-digit]]
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[[Category: pad]]
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[[Category: polymerase]]
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[[Category: rev1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:17:23 2007''
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Current revision

Ternary complex of the catalytic core of REV1 with DNA and dCTP.

PDB ID 2aq4

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