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| | <StructureSection load='3aiz' size='340' side='right'caption='[[3aiz]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3aiz' size='340' side='right'caption='[[3aiz]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aiz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AIZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aiz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AIZ 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></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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aix|3aix]]</div></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">st0397 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO]), st0944 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</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=3aiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aiz OCA], [https://pdbe.org/3aiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aiz RCSB], [https://www.ebi.ac.uk/pdbsum/3aiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aiz 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=3aiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aiz OCA], [https://pdbe.org/3aiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aiz RCSB], [https://www.ebi.ac.uk/pdbsum/3aiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aiz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PCNA2_SULTO PCNA2_SULTO]] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5' and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the Holliday junction cleavage enzyme.[HAMAP-Rule:MF_00317]<ref>PMID:18782564</ref> [[https://www.uniprot.org/uniprot/PCNA3_SULTO PCNA3_SULTO]] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5' and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the Holliday junction cleavage enzyme.[HAMAP-Rule:MF_00317]<ref>PMID:18782564</ref>
| + | [https://www.uniprot.org/uniprot/PCNA2_SULTO PCNA2_SULTO] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5' and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the Holliday junction cleavage enzyme.[HAMAP-Rule:MF_00317]<ref>PMID:18782564</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulto]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Higuchi, S]] | + | [[Category: Higuchi S]] |
| - | [[Category: Kawai, A]] | + | [[Category: Kawai A]] |
| - | [[Category: Miyamoto, S]] | + | [[Category: Miyamoto S]] |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Replication]]
| + | |
| Structural highlights
Function
PCNA2_SULTO Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5' and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the Holliday junction cleavage enzyme.[HAMAP-Rule:MF_00317][1]
Publication Abstract from PubMed
Proliferating cell nuclear antigen (PCNA) is a key protein that orchestrates the arrangement of DNA-processing proteins on DNA during DNA metabolism. In crenarchaea, PCNA forms a heterotrimer (PCNA123) consisting of PCNA1, PCNA2, and PCNA3, while in most eukaryotes and many archaea PCNAs form a homotrimer. Interestingly, unique oligomeric PCNAs from Sulfolobus tokodaii were reported in which PCNA2 and PCNA3 form a heterotrimer without PCNA1. In this paper, we describe the crystal structure of the stoPCNA2-stoPCNA3 complex. While most DNA sliding clamps form ring-shaped structures, our crystal structure showed an elliptic ring-like heterotetrameric complex, differing from a previous reports. Furthermore, we investigated the composition and the dimension of the stoPCNA2-stoPCNA3 complex in the solution using gel-filtration column chromatography and small-angle X-ray scattering analyses, respectively. These results indicate that stoPCNA2 and stoPCNA3 form the heterotetramer in solution. Based on our heterotetrameric structure, we propose a possible biological role for the heterotetrameric complex as a Holliday junction clamp.
A novel heterotetrameric structure of the crenarchaeal PCNA2-PCNA3 complex.,Kawai A, Hashimoto H, Higuchi S, Tsunoda M, Sato M, Nakamura KT, Miyamoto S J Struct Biol. 2011 Jun;174(3):443-50. Epub 2011 Feb 23. PMID:21352919[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lu S, Li Z, Wang Z, Ma X, Sheng D, Ni J, Shen Y. Spatial subunit distribution and in vitro functions of the novel trimeric PCNA complex from Sulfolobus tokodaii. Biochem Biophys Res Commun. 2008 Nov 14;376(2):369-74. doi:, 10.1016/j.bbrc.2008.08.150. Epub 2008 Sep 7. PMID:18782564 doi:http://dx.doi.org/10.1016/j.bbrc.2008.08.150
- ↑ Kawai A, Hashimoto H, Higuchi S, Tsunoda M, Sato M, Nakamura KT, Miyamoto S. A novel heterotetrameric structure of the crenarchaeal PCNA2-PCNA3 complex. J Struct Biol. 2011 Jun;174(3):443-50. Epub 2011 Feb 23. PMID:21352919 doi:10.1016/j.jsb.2011.02.006
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