6o09: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6o09' size='340' side='right'caption='[[6o09]], [[Resolution|resolution]] 2.06Å' scene=''> | <StructureSection load='6o09' size='340' side='right'caption='[[6o09]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6o09]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6o09]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O09 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o09 OCA], [https://pdbe.org/6o09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o09 RCSB], [https://www.ebi.ac.uk/pdbsum/6o09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o09 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 6o09" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6o09" 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: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Glycine max]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Couture | [[Category: Couture JF]] | ||
[[Category: Davarinejad | [[Category: Davarinejad H]] | ||
Latest revision as of 10:02, 11 October 2023
Structure of AtPCNA in complex with the PIP motif of ATXR6Structure of AtPCNA in complex with the PIP motif of ATXR6
Structural highlights
FunctionPCNA1_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] Publication Abstract from PubMedThe proliferating cell nuclear antigen (PCNA) is a sliding clamp associated with DNA polymerases and serves as a binding platform for the recruitment of regulatory proteins linked to DNA damage repair, cell cycle regulation, and epigenetic signaling. The histone H3 lysine-27 (H3K27) mono-methyltransferase Arabidopsis trithorax-related protein 5/6 (ATXR5/6) associates with PCNA, and this interaction has been proposed to act as a key determinant controlling the reestablishment of H3K27 mono-methylation following replication. In this study, we provide biochemical evidence showing that PCNA inhibits ATXR6 enzymatic activity. The structure of the ATXR6 PCNA-interacting peptide (PIP) in complex with PCNA indicates that a trio of hydrophobic residues contributes to the binding of the enzyme to the sliding clamp. Finally, despite the presence of three PIP binding clefts, only two molecules of ATXR6 bind to PCNA likely enabling the recruitment of a third protein to the sliding clamp. Collectively, these results rule out the model wherein PCNA-bound ATXR6 actively reestablishes H3K27 mono-methylation following DNA replication and provides insights into the role of ATXR6 PIP motif in its interaction with PCNA. ATXR5/6 Forms Alternative Protein Complexes with PCNA and the Nucleosome Core Particle.,Davarinejad H, Joshi M, Ait-Hamou N, Munro K, Couture JF J Mol Biol. 2019 Feb 28. pii: S0022-2836(19)30097-X. doi:, 10.1016/j.jmb.2019.02.020. PMID:30826376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||