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==Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit==
==Crystal Structure of human Pol alpha B-subunit in complex with C-terminal domain of catalytic subunit==
<StructureSection load='4y97' size='340' side='right' caption='[[4y97]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='4y97' size='340' side='right'caption='[[4y97]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4y97]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y97 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4y97]] is a 8 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=4Y97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y97 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.51&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4y97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y97 OCA], [http://pdbe.org/4y97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y97 RCSB], [http://www.ebi.ac.uk/pdbsum/4y97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y97 ProSAT]</span></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=4y97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y97 OCA], [https://pdbe.org/4y97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y97 RCSB], [https://www.ebi.ac.uk/pdbsum/4y97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y97 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DPOA2_HUMAN DPOA2_HUMAN]] May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery (By similarity). [[http://www.uniprot.org/uniprot/DPOLA_HUMAN DPOLA_HUMAN]] Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes.<ref>PMID:9518481</ref> 
[https://www.uniprot.org/uniprot/DPOA2_HUMAN DPOA2_HUMAN] May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery (By similarity).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4y97" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4y97" style="background-color:#fffaf0;"></div>
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed DNA polymerase]]
[[Category: Homo sapiens]]
[[Category: Babayeva, N D]]
[[Category: Large Structures]]
[[Category: Baranovskiy, A G]]
[[Category: Babayeva ND]]
[[Category: Gu, J]]
[[Category: Baranovskiy AG]]
[[Category: Suwa, Y]]
[[Category: Gu J]]
[[Category: Tahirov, T H]]
[[Category: Suwa Y]]
[[Category: Human dna polymerase alpha]]
[[Category: Tahirov TH]]
[[Category: Transferase]]

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