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| | ==Structure of sumoylated PCNA== | | ==Structure of sumoylated PCNA== |
| - | <StructureSection load='3pge' size='340' side='right' caption='[[3pge]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3pge' size='340' side='right'caption='[[3pge]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pge]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PGE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pge]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l0x|3l0x]]</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='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=3pge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pge OCA], [http://pdbe.org/3pge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pge RCSB], [http://www.ebi.ac.uk/pdbsum/3pge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pge 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=3pge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pge OCA], [https://pdbe.org/3pge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pge RCSB], [https://www.ebi.ac.uk/pdbsum/3pge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pge ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations. [[http://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST]] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref> | + | [https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.[https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3pge" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3pge" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker's yeast]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Brogie, J E]] | + | [[Category: Brogie JE]] |
| - | [[Category: Freudenthal, B D]] | + | [[Category: Freudenthal BD]] |
| - | [[Category: Gakhar, L]] | + | [[Category: Gakhar L]] |
| - | [[Category: Washington, T]] | + | [[Category: Washington T]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna replication]]
| + | |
| Structural highlights
Function
SMT3_YEAST Not known; suppressor of MIF2 mutations.PCNA_YEAST This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.[1] [2]
Publication Abstract from PubMed
Eukaryotic proliferating cell nuclear antigen (PCNA) is a replication accessory protein that functions in DNA replication, repair, and recombination. The various functions of PCNA are regulated by posttranslational modifications including mono-ubiquitylation, which promotes translesion synthesis, and sumoylation, which inhibits recombination. To understand how SUMO modification regulates PCNA, we generated a split SUMO-modified PCNA protein and showed that it supports cell viability and stimulates DNA polymerase delta activity. We then determined its X-ray crystal structure and found that SUMO occupies a position on the back face of the PCNA ring, which is distinct from the position occupied by ubiquitin in the structure of ubiquitin-modified PCNA. We propose that the back of PCNA has evolved to be a site of regulation that can be easily modified without disrupting ongoing reactions on the front of PCNA, such as normal DNA replication. Moreover, these modifications likely allow PCNA to function as a tool belt, whereby proteins can be recruited to the replication machinery via the back of PCNA and be held in reserve until needed.
Crystal Structure of SUMO-Modified Proliferating Cell Nuclear Antigen.,Freudenthal BD, Brogie JE, Gakhar L, Kondratick CM, Washington MT J Mol Biol. 2010 Dec 15. PMID:21167178[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Haracska L, Kondratick CM, Unk I, Prakash S, Prakash L. Interaction with PCNA is essential for yeast DNA polymerase eta function. Mol Cell. 2001 Aug;8(2):407-15. PMID:11545742
- ↑ Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 2002 Sep 12;419(6903):135-41. PMID:12226657 doi:10.1038/nature00991
- ↑ Freudenthal BD, Brogie JE, Gakhar L, Kondratick CM, Washington MT. Crystal Structure of SUMO-Modified Proliferating Cell Nuclear Antigen. J Mol Biol. 2010 Dec 15. PMID:21167178 doi:10.1016/j.jmb.2010.12.015
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