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==Crystal structure of PCNA12 dimer from Sulfolobus solfataricus.==
==Crystal structure of PCNA12 dimer from Sulfolobus solfataricus.==
<StructureSection load='2io4' size='340' side='right' caption='[[2io4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2io4' size='340' side='right'caption='[[2io4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2io4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IO4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2io4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IO4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ijx|2ijx]], [[2izo|2izo]], [[2ix2|2ix2]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcnB, pcnA-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO]), pcnC, pcnA-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</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=2io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2io4 OCA], [https://pdbe.org/2io4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2io4 RCSB], [https://www.ebi.ac.uk/pdbsum/2io4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2io4 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2io4 OCA], [http://pdbe.org/2io4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2io4 RCSB], [http://www.ebi.ac.uk/pdbsum/2io4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2io4 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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2io4 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2io4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA sliding clamps form an oligomeric ring encircling DNA and serve as a moving platform for DNA-processing proteins. The opening and closing of a sliding-clamp ring is essential to load the clamp onto DNA in order to perform its functions. The molecular details of how clamp rings open and enclose DNA are still not clear. Three PCNA homologues have been found in Sulfolobus solfataricus which form a heterotrimer. Taking advantage of their hetero-oligomeric nature, the structures of the PCNAs in monomeric PCNA3, dimeric PCNA1-PCNA2 and trimeric PCNA1-PCNA2-PCNA3 forms were determined at resolutions of 2.6-1.9 A. The distinct oligomeric structures represent different stages in ring formation, which were verified in solution by ultracentrifugation analysis. The heterodimer opens in a V-shape of 130 degrees , while the heterotrimers form a ring with a 120 degrees rotation between monomers. The association of a rigid PCNA3 monomer with an opened PCNA1-PCNA2 heterodimer closes the ring and introduces a spring tension in the PCNA1-PCNA2 interface, thus bending the nine-stranded intermolecular beta-sheet to fit the 120 degrees rotation. The release of the spring tension as PCNA3 dissociates from the ring may facilitate ring opening. The structural features in different assemblies present a molecular model for clamp ring assembly and opening.
Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening.,Hlinkova V, Xing G, Bauer J, Shin YJ, Dionne I, Rajashankar KR, Bell SD, Ling H Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):941-9. Epub 2008, Aug 13. PMID:18703842<ref>PMID:18703842</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2io4" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Proliferating Cell Nuclear Antigen|Proliferating Cell Nuclear Antigen]]
*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Sulso]]
[[Category: Large Structures]]
[[Category: Hlinkova, V]]
[[Category: Saccharolobus solfataricus P2]]
[[Category: Ling, H]]
[[Category: Hlinkova V]]
[[Category: Dna binding protein]]
[[Category: Ling H]]
[[Category: Pcna12 heterodimer]]
[[Category: Pcna123 heterotrimer]]
[[Category: Protein-protein interaction]]

Latest revision as of 12:03, 21 February 2024

Crystal structure of PCNA12 dimer from Sulfolobus solfataricus.Crystal structure of PCNA12 dimer from Sulfolobus solfataricus.

Structural highlights

2io4 is a 4 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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
  2. ↑ 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

2io4, resolution 2.60Å

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