9f28
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the heterodimeric primase from pyrococcus abyssi (deletion of the PriL-CTD domain)== | |
| - | + | <StructureSection load='9f28' size='340' side='right'caption='[[9f28]], [[Resolution|resolution]] 1.85Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9f28]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9F28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F28 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9f28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f28 OCA], [https://pdbe.org/9f28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f28 RCSB], [https://www.ebi.ac.uk/pdbsum/9f28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f28 ProSAT]</span></td></tr> |
| - | [[Category: Madru | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRIS_PYRAB PRIS_PYRAB] 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, synthesizing DNA strands up to 3 kB. 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 for RNA fragments up to 150 bases. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Displays gap-filling and strand-displacement activities.<ref>PMID:17991487</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus abyssi]] | ||
| + | [[Category: Madru C]] | ||
| + | [[Category: Sauguet L]] | ||
Current revision
Crystal structure of the heterodimeric primase from pyrococcus abyssi (deletion of the PriL-CTD domain)
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