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| | <StructureSection load='2ix2' size='340' side='right'caption='[[2ix2]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2ix2' size='340' side='right'caption='[[2ix2]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ix2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IX2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ix2]] is a 3 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=2IX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2izo|2izo]]</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]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ix2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix2 OCA], [http://pdbe.org/2ix2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ix2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ix2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix2 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=2ix2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix2 OCA], [https://pdbe.org/2ix2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PCNA2_SULSO PCNA2_SULSO]] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [[http://www.uniprot.org/uniprot/PCNA3_SULSO PCNA3_SULSO]] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity). | + | [https://www.uniprot.org/uniprot/PCNA1_SACS2 PCNA1_SACS2] One of the sliding clamp subunits that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Heterotrimer stimulates the Holliday junction resolvase Hjc. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.<ref>PMID:12535540</ref> <ref>PMID:17011573</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> |
| - | [[Category: Saccharolobus solfataricus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carter, L]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Johnson, K]] | + | [[Category: Carter L]] |
| - | [[Category: Liu, H]] | + | [[Category: Johnson K]] |
| - | [[Category: McMahon, S A]] | + | [[Category: Liu H]] |
| - | [[Category: Naismith, J H]] | + | [[Category: McMahon SA]] |
| - | [[Category: Oke, M]] | + | [[Category: Naismith JH]] |
| - | [[Category: Taylor, G L]] | + | [[Category: Oke M]] |
| - | [[Category: White, M F]] | + | [[Category: Taylor GL]] |
| - | [[Category: Williams, G J]] | + | [[Category: White MF]] |
| - | [[Category: Dna replication]]
| + | [[Category: Williams GJ]] |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Pcna]]
| + | |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Sulfolobus sulfataricus]]
| + | |
| Structural highlights
Function
PCNA1_SACS2 One of the sliding clamp subunits that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Heterotrimer stimulates the Holliday junction resolvase Hjc. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.[1] [2]
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
PCNA is a ring-shaped protein that encircles DNA, providing a platform for the association of a wide variety of DNA-processing enzymes that utilize the PCNA sliding clamp to maintain proximity to their DNA substrates. PCNA is a homotrimer in eukaryotes, but a heterotrimer in crenarchaea such as Sulfolobus solfataricus. The three proteins are SsoPCNA1 (249 residues), SsoPCNA2 (245 residues) and SsoPCNA3 (259 residues). The heterotrimeric protein crystallizes in space group P2(1), with unit-cell parameters a = 44.8, b = 78.8, c = 125.6 A, beta = 100.5 degrees. The crystal structure of this heterotrimeric PCNA molecule has been solved using molecular replacement. The resulting structure to 2.3 A sheds light on the differential stabilities of the interactions observed between the three subunits and the specificity of individual subunits for partner proteins.
Structure of the heterotrimeric PCNA from Sulfolobus solfataricus.,Williams GJ, Johnson K, Rudolf J, McMahon SA, Carter L, Oke M, Liu H, Taylor GL, White MF, Naismith JH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):944-8. Epub 2006 Sep 19. PMID:17012780[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dionne I, Nookala RK, Jackson SP, Doherty AJ, Bell SD. A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol Cell. 2003 Jan;11(1):275-82. PMID:12535540 doi:10.1016/s1097-2765(02)00824-9
- ↑ Dorazi R, Parker JL, White MF. PCNA activates the Holliday junction endonuclease Hjc. J Mol Biol. 2006 Dec 1;364(3):243-7. Epub 2006 Sep 9. PMID:17011573 doi:http://dx.doi.org/10.1016/j.jmb.2006.09.011
- ↑ Williams GJ, Johnson K, Rudolf J, McMahon SA, Carter L, Oke M, Liu H, Taylor GL, White MF, Naismith JH. Structure of the heterotrimeric PCNA from Sulfolobus solfataricus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):944-8. Epub 2006 Sep 19. PMID:17012780 doi:10.1107/S1744309106034075
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