3ja9: Difference between revisions

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<SX load='3ja9' size='340' side='right' viewer='molstar' caption='[[3ja9]], [[Resolution|resolution]] 22.00&Aring;' scene=''>
<SX load='3ja9' size='340' side='right' viewer='molstar' caption='[[3ja9]], [[Resolution|resolution]] 22.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ja9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JA9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ja9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JA9 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCNA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 22&#8491;</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=3ja9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ja9 OCA], [https://pdbe.org/3ja9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ja9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ja9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ja9 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=3ja9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ja9 OCA], [https://pdbe.org/3ja9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ja9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ja9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ja9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PCNA_HUMAN PCNA_HUMAN]] 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. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.<ref>PMID:19443450</ref> <ref>PMID:18719106</ref> 
[https://www.uniprot.org/uniprot/PCNA_HUMAN PCNA_HUMAN] 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. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.<ref>PMID:19443450</ref> <ref>PMID:18719106</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Translesion synthesis (TLS) is the mechanism by which DNA polymerases replicate through unrepaired DNA lesions. TLS is activated by monoubiquitination of the homotrimeric proliferating cell nuclear antigen (PCNA) at lysine-164, followed by the switch from replicative to specialized polymerases at DNA damage sites. Pol eta belongs to the Y-Family of specialized polymerases that can efficiently bypass UV-induced lesions. Like other members of the Y-Family polymerases, its recruitment to the damaged sites is mediated by the interaction with monoubiquitinated PCNA (Ub-PCNA) via its ubiquitin-binding domain and non-canonical PCNA-interacting motif in the C-terminal region. The structural determinants underlying the direct recognition of Ub-PCNA by Pol eta, or Y-Family polymerases in general, remain largely unknown. Here we report a structure of the Ub-PCNA/Pol eta complex bound to DNA determined by single-particle electron microscopy (EM). The overall obtained structure resembles that of the editing PCNA/PolB complex. Analysis of the map revealed the conformation of ubiquitin that binds the C-terminal domain of Pol eta. Our present study suggests that the Ub-PCNA/Pol eta interaction requires the formation of a structured binding interface, which is dictated by the inherent flexibility of Ub-PCNA.
 
Molecular architecture of the Ub-PCNA/Pol eta complex bound to DNA.,Lau WC, Li Y, Zhang Q, Huen MS Sci Rep. 2015 Oct 27;5:15759. doi: 10.1038/srep15759. PMID:26503230<ref>PMID:26503230</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ja9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Huen, M S.Y]]
[[Category: Huen MSY]]
[[Category: Lau, W C.Y]]
[[Category: Lau WCY]]
[[Category: Li, Y]]
[[Category: Li Y]]
[[Category: Zhang, Q]]
[[Category: Zhang Q]]
[[Category: Dna]]
[[Category: Dna binding protein]]
[[Category: Dna-binding systemic lupus erythematosus]]
[[Category: Oncogene]]
[[Category: Processivity]]
[[Category: Replication]]

Revision as of 08:41, 7 February 2024

Structure of native human PCNA

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