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2m2i

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{{STRUCTURE_2m2i| PDB=2m2i | SCENE= }}
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==NMR solution structure of BRCT domain of yeast REV1==
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===NMR solution structure of BRCT domain of yeast REV1===
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<StructureSection load='2m2i' size='340' side='right' caption='[[2m2i]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_23747975}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2m2i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M2I FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">REV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<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=2m2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m2i RCSB], [http://www.ebi.ac.uk/pdbsum/2m2i PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Function==
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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>
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[[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>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2m2i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2I OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:023747975</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
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[[Category: Korzhnev, D M.]]
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[[Category: Korzhnev, D M]]
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[[Category: Maciejewski, M W.]]
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[[Category: Maciejewski, M W]]
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[[Category: Pustovalova, Y.]]
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[[Category: Pustovalova, Y]]
[[Category: Brct]]
[[Category: Brct]]
[[Category: Rev1]]
[[Category: Rev1]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 04:52, 22 December 2014

NMR solution structure of BRCT domain of yeast REV1

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