4fxd: Difference between revisions
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==Crystal structure of yeast DNA polymerase alpha bound to DNA/RNA== | ==Crystal structure of yeast DNA polymerase alpha bound to DNA/RNA== | ||
<StructureSection load='4fxd' size='340' side='right' caption='[[4fxd]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4fxd' size='340' side='right' caption='[[4fxd]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC17, N2181, POL1, YNL102W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC17, N2181, POL1, YNL102W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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='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=4fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fxd RCSB], [http://www.ebi.ac.uk/pdbsum/4fxd PDBsum]</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=4fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxd OCA], [http://pdbe.org/4fxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fxd RCSB], [http://www.ebi.ac.uk/pdbsum/4fxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4fxd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 18:01, 4 August 2016
Crystal structure of yeast DNA polymerase alpha bound to DNA/RNACrystal structure of yeast DNA polymerase alpha bound to DNA/RNA
Structural highlights
Function[DPOA_YEAST] Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.[1] Publication Abstract from PubMedThe DNA Polymerase alpha (Pol alpha)/primase complex initiates DNA synthesis in eukaryotic replication. In the complex, Pol alpha and primase cooperate in the production of RNA-DNA oligonucleotides that prime synthesis of new DNA. Here we report crystal structures of the catalytic core of yeast Pol alpha in unliganded form, bound to an RNA primer/DNA template and extending an RNA primer with deoxynucleotides. We combine the structural analysis with biochemical and computational data to demonstrate that Pol alpha specifically recognizes the A-form RNA/DNA helix and that the ensuing synthesis of B-form DNA terminates primer synthesis. The spontaneous release of the completed RNA-DNA primer by the Pol alpha/primase complex simplifies current models of primer transfer to leading- and lagging strand polymerases. The proposed mechanism of nucleotide polymerization by Pol alpha might contribute to genomic stability by limiting the amount of inaccurate DNA to be corrected at the start of each Okazaki fragment. DOI:http://dx.doi.org/10.7554/eLife.00482.001. Mechanism for priming DNA synthesis by yeast DNA Polymerase alpha.,Perera RL, Torella R, Klinge S, Kilkenny ML, Maman JD, Pellegrini L Elife. 2013 Apr 2;2:e00482. doi: 10.7554/eLife.00482. Print 2013. PMID:23599895[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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