4fxd: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fxd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXD FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fxd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXD FirstGlance]. <br>
</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=4fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxd OCA], [https://pdbe.org/4fxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxd RCSB], [https://www.ebi.ac.uk/pdbsum/4fxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxd ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=4fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxd OCA], [https://pdbe.org/4fxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxd RCSB], [https://www.ebi.ac.uk/pdbsum/4fxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/DPOLA_YEAST DPOLA_YEAST] Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849). POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).<ref>PMID:10898792</ref> <ref>PMID:22119860</ref> <ref>PMID:31488849</ref>  
[https://www.uniprot.org/uniprot/DPOLA_YEAST DPOLA_YEAST] Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849). POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).<ref>PMID:10898792</ref> <ref>PMID:22119860</ref> <ref>PMID:31488849</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:23599895</ref>
==See Also==
 
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fxd" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 18:35, 14 March 2024

Crystal structure of yeast DNA polymerase alpha bound to DNA/RNACrystal structure of yeast DNA polymerase alpha bound to DNA/RNA

Structural highlights

4fxd is a 6 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPOLA_YEAST Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849). POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).[1] [2] [3]

See Also

References

  1. ↑ Qi H, Zakian VA. The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein. Genes Dev. 2000 Jul 15;14(14):1777-88. PMID:10898792
  2. ↑ Netz DJ, Stith CM, Stumpfig M, Kopf G, Vogel D, Genau HM, Stodola JL, Lill R, Burgers PM, Pierik AJ. Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes. Nat Chem Biol. 2011 Nov 27;8(1):125-32. doi: 10.1038/nchembio.721. PMID:22119860 doi:http://dx.doi.org/10.1038/nchembio.721
  3. ↑ Zhou ZX, Lujan SA, Burkholder AB, Garbacz MA, Kunkel TA. Roles for DNA polymerase delta in initiating and terminating leading strand DNA replication. Nat Commun. 2019 Sep 5;10(1):3992. doi: 10.1038/s41467-019-11995-z. PMID:31488849 doi:http://dx.doi.org/10.1038/s41467-019-11995-z

4fxd, resolution 3.00Å

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