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{{STRUCTURE_2m2i|  PDB=2m2i  |  SCENE=  }}
===NMR solution structure of BRCT domain of yeast REV1===
{{ABSTRACT_PUBMED_23747975}}


==Function==
==NMR solution structure of BRCT domain of yeast REV1==
[[http://www.uniprot.org/uniprot/REV1_YEAST REV1_YEAST]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.<ref>PMID:8751446</ref> <ref>PMID:11316789</ref> <ref>PMID:16452144</ref>
<StructureSection load='2m2i' size='340' side='right'caption='[[2m2i]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m2i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M2I FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2i OCA], [https://pdbe.org/2m2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m2i RCSB], [https://www.ebi.ac.uk/pdbsum/2m2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m2i ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/REV1_YEAST REV1_YEAST] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.<ref>PMID:8751446</ref> <ref>PMID:11316789</ref> <ref>PMID:16452144</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rev1 is a Y-family translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap filling. In the process of TLS, high-fidelity replicative DNA polymerases stalled by DNA damage are replaced by error-prone TLS enzymes responsible for the majority of mutagenesis in eukaryotic cells. The polymerase exchange that gains low-fidelity TLS polymerases access to DNA is mediated by their interactions with proliferating cell nuclear antigen (PCNA). Rev1 stands alone from other Y-family TLS enzymes since it lacks the consensus PCNA-interacting protein box (PIP-box) motif, instead utilizing other modular domains for PCNA binding. Here we report solution NMR structure of an 11-kDa BRCA1 C-terminus (BRCT) domain from Saccharomyces cerevisiae Rev1 and demonstrate with the use of transverse relaxation optimized spectroscopy NMR methods that Rev1-BRCT domain directly interacts with an 87-kDa PCNA in solution. The domain adopts alpha/beta fold (beta1-alpha1-beta2-beta3-alpha2-beta4-alpha3-alpha4) typical for BRCT domain superfamily. PCNA-binding interface of the Rev1-BRCT domain comprises conserved residues of the outer surface of the alpha1 helix and the alpha1-beta1, beta2-beta3 and beta3-alpha2 loops. On the other hand, Rev1-BRCT binds to the inter-domain region of PCNA that overlaps with the binding site for the PIP-box motif. Furthermore, Rev1-BRCT domain bound to PCNA can be displaced by increasing amounts of the PIP-box peptide from TLS DNA polymerase poleta, suggesting that Rev1-BRCT and poleta PIP-box interactions with the same PCNA monomer are mutually exclusive. These results provide structural insights into PCNA recognition by TLS DNA polymerases that help better understand TLS regulation in eukaryotes.


==About this Structure==
NMR Mapping of PCNA Interaction with Translesion Synthesis DNA Polymerase Rev1 Mediated by Rev1-BRCT Domain.,Pustovalova Y, Maciejewski MW, Korzhnev DM J Mol Biol. 2013 Jun 7. pii: S0022-2836(13)00359-8. doi:, 10.1016/j.jmb.2013.05.029. PMID:23747975<ref>PMID:23747975</ref>
[[2m2i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2I OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023747975</ref><references group="xtra"/><references/>
</div>
[[Category: Korzhnev, D M.]]
<div class="pdbe-citations 2m2i" style="background-color:#fffaf0;"></div>
[[Category: Maciejewski, M W.]]
 
[[Category: Pustovalova, Y.]]
==See Also==
[[Category: Brct]]
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
[[Category: Rev1]]
== References ==
[[Category: Transferase]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Korzhnev DM]]
[[Category: Maciejewski MW]]
[[Category: Pustovalova Y]]
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