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| <StructureSection load='2zvv' size='340' side='right'caption='[[2zvv]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2zvv' size='340' side='right'caption='[[2zvv]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2zvv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZVV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zvv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZVV 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]] 2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zvw|2zvw]]</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvv OCA], [http://pdbe.org/2zvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zvv RCSB], [http://www.ebi.ac.uk/pdbsum/2zvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvv 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=2zvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvv OCA], [https://pdbe.org/2zvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvv RCSB], [https://www.ebi.ac.uk/pdbsum/2zvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvv ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/PCNA1_ARATH PCNA1_ARATH]] 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 (By similarity).[HAMAP-Rule:MF_00317] [[http://www.uniprot.org/uniprot/CDN1A_HUMAN CDN1A_HUMAN]] May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex.<ref>PMID:8242751</ref> <ref>PMID:9106657</ref> | + | [https://www.uniprot.org/uniprot/PCNA1_ARATH PCNA1_ARATH] 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 (By similarity).[HAMAP-Rule:MF_00317] |
| == 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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Morikawa, K]] | + | [[Category: Morikawa K]] |
- | [[Category: Oyama, T]] | + | [[Category: Oyama T]] |
- | [[Category: Strzalka, W]] | + | [[Category: Strzalka W]] |
- | [[Category: Tori, K]] | + | [[Category: Tori K]] |
- | [[Category: Dna binding protein]]
| + | |
- | [[Category: Dna replication]]
| + | |
- | [[Category: Dna-binding]]
| + | |
- | [[Category: Nucleus]]
| + | |
- | [[Category: Protein-peptide complex]]
| + | |
| Structural highlights
Function
PCNA1_ARATH 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 (By similarity).[HAMAP-Rule:MF_00317]
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
The proliferating cell nuclear antigen (PCNA) is well recognized as one of the essential cellular components of the DNA replication machinery in all eukaryotic organisms. Despite their prominent importance, very little biochemical and structural information about plant PCNAs is available, in comparison with that obtained from other eukaryotic organisms. We have determined the atomic resolution crystal structures of the two distinct Arabidopsis thaliana PCNAs (AtPCNA), both complexed with the C-terminal segment of human p21. Both AtPCNAs form homotrimeric ring structures, which are essentially identical to each other, including the major contacts with the p21 peptide. The structure of the amino-terminal half of the p21 peptide, containing the typical PIP box sequence, is remarkably similar to those observed in the previously reported crystal structures of the human and archaeal PCNA-PIP box complexes. Meanwhile, the carboxy-terminal halves of the p21 peptide in the plant PCNA complexes are bound to the protein in a unique manner, most probably because of crystal packing effects. A surface plasmon resonance analysis revealed high affinity between each AtPCNA and the C-terminal fragment of human p21. This result strongly suggests that the interaction is functionally significant, although no plant homologs of p21 have been identified yet. We also discovered that AtPCNA1 and AtPCNA2 form heterotrimers, implying that hetero-PCNA rings may play critical roles in cellular signal transduction, particularly in DNA repair.
Crystal structures of the Arabidopsis thaliana proliferating cell nuclear antigen 1 and 2 proteins complexed with the human p21 C-terminal segment.,Strzalka W, Oyama T, Tori K, Morikawa K Protein Sci. 2009 May;18(5):1072-80. PMID:19388052[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Strzalka W, Oyama T, Tori K, Morikawa K. Crystal structures of the Arabidopsis thaliana proliferating cell nuclear antigen 1 and 2 proteins complexed with the human p21 C-terminal segment. Protein Sci. 2009 May;18(5):1072-80. PMID:19388052 doi:10.1002/pro.117
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