|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1zt2' size='340' side='right'caption='[[1zt2]], [[Resolution|resolution]] 3.33Å' scene=''> | | <StructureSection load='1zt2' size='340' side='right'caption='[[1zt2]], [[Resolution|resolution]] 3.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zt2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZT2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zt2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZT2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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]] 3.33Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">priA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 'Saccharolobus solfataricus']), priB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 'Saccharolobus solfataricus'])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1zt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zt2 OCA], [https://pdbe.org/1zt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zt2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zt2 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=1zt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zt2 OCA], [https://pdbe.org/1zt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zt2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zt2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PRIS_SULSO PRIS_SULSO]] 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. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.<ref>PMID:15561142</ref> [[https://www.uniprot.org/uniprot/PRIL_SULSO PRIL_SULSO]] Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, 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. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.<ref>PMID:15561142</ref>
| + | [https://www.uniprot.org/uniprot/PRIS_SACS2 PRIS_SACS2] 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. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.[HAMAP-Rule:MF_00700]<ref>PMID:15561142</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 36: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Saccharolobus solfataricus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bell, S D]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Lao-Sirieix, S H]] | + | [[Category: Bell SD]] |
| - | [[Category: Nookala, R K]] | + | [[Category: Lao-Sirieix SH]] |
| - | [[Category: Pellegrini, L]] | + | [[Category: Nookala RK]] |
| - | [[Category: Roversi, P]] | + | [[Category: Pellegrini L]] |
| - | [[Category: Heterodimeric complex]]
| + | [[Category: Roversi P]] |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PRIS_SACS2 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. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.[HAMAP-Rule:MF_00700][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Primases are DNA-dependent RNA polymerases that synthesize the oligoribonucleotide primers essential to DNA replication. In archaeal and eukaryotic organisms, the core primase is a heterodimeric enzyme composed of a small and a large subunit. Here we report a crystallographic and biochemical analysis of the core primase from the archaeon Sulfolobus solfataricus. The structure provides the first three-dimensional description of the large subunit and its interaction with the small subunit. The evolutionary conservation of amino acids at the protein-protein interface implies that the observed mode of subunit association is conserved among archaeal and eukaryotic primases. The orientation of the large subunit in the core primase probably excludes its direct involvement in catalysis. Modeling of a DNA-RNA helix together with structure-based site-directed mutagenesis provides insight into the mechanism of template DNA binding and RNA primer synthesis.
Structure of the heterodimeric core primase.,Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L Nat Struct Mol Biol. 2005 Dec;12(12):1137-44. Epub 2005 Nov 6. PMID:16273105[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lao-Sirieix SH, Bell SD. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities. J Mol Biol. 2004 Dec 10;344(5):1251-63. PMID:15561142 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.018
- ↑ Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L. Structure of the heterodimeric core primase. Nat Struct Mol Biol. 2005 Dec;12(12):1137-44. Epub 2005 Nov 6. PMID:16273105 doi:10.1038/nsmb1013
|
