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| | ==Structure of split monoubiquitinated PCNA with ubiquitin in position one== | | ==Structure of split monoubiquitinated PCNA with ubiquitin in position one== |
| - | <StructureSection load='3l10' size='340' side='right' caption='[[3l10]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3l10' size='340' side='right'caption='[[3l10]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3l10]] 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=3L10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L10 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l10]] 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=3L10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L10 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l0w|3l0w]], [[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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">POL30, YBR0811, YBR088C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), POL30, Pol30 & UBI1, YBR0811, YBR088C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l10 OCA], [https://pdbe.org/3l10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l10 RCSB], [https://www.ebi.ac.uk/pdbsum/3l10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l10 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=3l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l10 OCA], [http://pdbe.org/3l10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l10 RCSB], [http://www.ebi.ac.uk/pdbsum/3l10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l10 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3l10" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3l10" 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: Freudenthal, B D]] | + | [[Category: Freudenthal BD]] |
| - | [[Category: Gakhar, L]] | + | [[Category: Gakhar L]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Washington, M T]] | + | [[Category: Washington MT]] |
| - | [[Category: Dna damage]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Isopeptide bond]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Ubl conjugation]]
| + | |
| Structural highlights
Function
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]
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
DNA synthesis by classical polymerases can be blocked by many lesions. These blocks are overcome by translesion synthesis, whereby the stalled classical, replicative polymerase is replaced by a nonclassical polymerase. In eukaryotes this polymerase exchange requires proliferating cell nuclear antigen (PCNA) monoubiquitination. To better understand the polymerase exchange, we developed a means of producing monoubiquitinated PCNA, by splitting the protein into two self-assembling polypeptides. We determined the X-ray crystal structure of monoubiquitinated PCNA and found that the ubiquitin moieties are located on the back face of PCNA and interact with it through their canonical hydrophobic surface. Moreover, the attachment of ubiquitin does not change PCNA's conformation. We propose that PCNA ubiquitination facilitates nonclassical polymerase recruitment to the back of PCNA by forming a new binding surface for nonclassical polymerases, consistent with a 'tool belt' model of the polymerase exchange.
Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange.,Freudenthal BD, Gakhar L, Ramaswamy S, Washington MT Nat Struct Mol Biol. 2010 Apr;17(4):479-84. Epub 2010 Mar 21. PMID:20305653[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, Gakhar L, Ramaswamy S, Washington MT. Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange. Nat Struct Mol Biol. 2010 Apr;17(4):479-84. Epub 2010 Mar 21. PMID:20305653 doi:10.1038/nsmb.1776
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