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1v34

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Current revision (23:57, 27 December 2023) (edit) (undo)
 
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<StructureSection load='1v34' size='340' side='right'caption='[[1v34]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1v34' size='340' side='right'caption='[[1v34]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1v34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V34 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1v34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V34 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v33|1v33]]</div></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=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1v34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v34 OCA], [https://pdbe.org/1v34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v34 RCSB], [https://www.ebi.ac.uk/pdbsum/1v34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v34 ProSAT], [https://www.topsan.org/Proteins/RSGI/1v34 TOPSAN]</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=1v34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v34 OCA], [https://pdbe.org/1v34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v34 RCSB], [https://www.ebi.ac.uk/pdbsum/1v34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v34 ProSAT], [https://www.topsan.org/Proteins/RSGI/1v34 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PRIS_PYRHO PRIS_PYRHO]] Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.<ref>PMID:14750947</ref>
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[https://www.uniprot.org/uniprot/PRIS_PYRHO PRIS_PYRHO] Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.<ref>PMID:14750947</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pyrococcus shinkaii]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hanaoka, F]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Ito, N]]
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[[Category: Hanaoka F]]
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[[Category: Nureki, O]]
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[[Category: Ito N]]
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[[Category: Structural genomic]]
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[[Category: Nureki O]]
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[[Category: Shirouzu, M]]
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[[Category: Shirouzu M]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Nucleotidyl transferase]]
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[[Category: Rsgi]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Pyrococcus horikoshii DNA primase-UTP complex

PDB ID 1v34

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