3rrg: Difference between revisions

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-[[Image:3rrg.png|left|200px]]
+==Ternary Structure of the large fragment of Taq DNA polymerase bound to an abasic site and a ddGTP==
+<StructureSection load='3rrg' size='340' side='right' caption='[[3rrg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3rrg]] is a 3 chain structure with 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=3RRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RRG FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DG3:2-3-DIDEOXYGUANOSINE-5-TRIPHOSPHATE'>DG3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=DDG:2,3-DIDEOXY-GUANOSINE-5-MONOPHOSPHATE'>DDG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lwl|3lwl]], [[3rr7|3rr7]], [[3rr8|3rr8]], [[3rrh|3rrh]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol I, pol1, polA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rrg RCSB], [http://www.ebi.ac.uk/pdbsum/3rrg PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cleavage of the N-glycosidic bond that connects the nucleobase to the backbone in DNA leads to abasic sites, the most frequent lesion under physiological conditions. Several DNA polymerases preferentially incorporate an A opposite this lesion, a phenomenon termed A-rule. Accordingly, KlenTaq, the large fragment of Thermus aquaticus DNA polymerase I, incorporates a nucleotide opposite an abasic with efficiencies of A &gt; G &gt; T &gt; C. Here we provide structural insights into constrains of the active site during nucleotide selection opposite an abasic site. It appears that these confines govern the nucleotide selection mainly by interaction of the incoming nucleotide with Tyr671. Depending on the nucleobase the nucleotides are differently positioned opposite Tyr671 resulting in different alignments of the functional groups that are required for bond formation. The distances between the alpha-phosphate and the 3'-primer terminus increases in the order A &lt; G &lt; T, which follows the order of incorporation efficiency. Additionally, a binary KlenTaq structure bound to DNA containing an abasic site indicates that binding of the nucleotide triggers a remarkable rearrangement of enzyme and DNA template. The ability to resolve the stacking arrangement might be dependent by the intrinsic properties of the respective nucleotide contributing to nucleotide selection. Furthermore, we studied the incorporation of a non-natural nucleotide opposite an abasic site. The nucleotide was often used in studying stacking effects in DNA polymerization. Here, no interaction with Tyr761 as found for the natural nucleotides is observed indicating a different reaction path for this non-natural nucleotide.
-{{STRUCTURE_3rrg|  PDB=3rrg  |  SCENE=  }}
+Amino acid templating mechanisms in selection of nucleotides opposite abasic sites by a family A DNA polymerase.,Obeid S, Welte W, Diederichs K, Marx A J Biol Chem. 2012 Feb 7. PMID:22318723<ref>PMID:22318723</ref>
-===Ternary Structure of the large fragment of Taq DNA polymerase bound to an abasic site and a ddGTP===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_22318723}}
-==About this Structure==
-[[3rrg]] is a 3 chain structure with 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=3RRG OCA].
 ==See Also==
 *[[DNA polymerase|DNA polymerase]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:022318723</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: DNA-directed DNA polymerase]]
 [[Category: Thermus aquaticus]]
-[[Category: Diederichs, K.]]
+[[Category: Diederichs, K]]
-[[Category: Marx, A.]]
+[[Category: Marx, A]]
-[[Category: Obeid, S.]]
+[[Category: Obeid, S]]
 [[Category: A-rule]]
 [[Category: Abasic site]]