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2l0g

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==Solution NMR structure of ubiquitin-binding motif (UBM2) of human polymerase iota==
==Solution NMR structure of ubiquitin-binding motif (UBM2) of human polymerase iota==
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<StructureSection load='2l0g' size='340' side='right' caption='[[2l0g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l0g' size='340' side='right'caption='[[2l0g]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l0g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L0G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0G FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l0f|2l0f]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l0g RCSB], [http://www.ebi.ac.uk/pdbsum/2l0g PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0g OCA], [https://pdbe.org/2l0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0g RCSB], [https://www.ebi.ac.uk/pdbsum/2l0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0g ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/POLI_HUMAN POLI_HUMAN] Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.<ref>PMID:11013228</ref> <ref>PMID:11251121</ref> <ref>PMID:11387224</ref> <ref>PMID:12410315</ref> <ref>PMID:14630940</ref> <ref>PMID:15199127</ref> <ref>PMID:15254543</ref>
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Cells have evolved mutagenic bypass mechanisms that prevent stalling of the replication machinery at DNA lesions. This process, translesion DNA synthesis (TLS), involves switching from high-fidelity DNA polymerases to specialized DNA polymerases that replicate through a variety of DNA lesions. In eukaryotes, polymerase switching during TLS is regulated by the DNA damage-triggered monoubiquitylation of PCNA. How the switch operates is unknown, but all TLS polymerases of the so-called Y-family possess PCNA and ubiquitin-binding domains that are important for their function. To gain insight into the structural mechanisms underlying the regulation of TLS by ubiquitylation, we have probed the interaction of ubiquitin with a conserved ubiquitin-binding motif (UBM2) of Y-family polymerase Poliota. Using NMR spectroscopy, we have determined the structure of a complex of human Poliota UBM2 and ubiquitin, revealing a novel ubiquitin recognition fold consisting of two alpha-helices separated by a central trans-proline residue conserved in all UBMs. We show that, different from the majority of ubiquitin complexes characterized to date, ubiquitin residue Ile44 only plays a modest role in the association of ubiquitin with Poliota UBM2. Instead, binding of UBM2 is centered on the recognition of Leu8 in ubiquitin, which is essential for the interaction.
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Structural Basis of Ubiquitin Recognition by Translesion Synthesis DNA Polymerase iota,Cui G, Benirschke RC, Tuan HF, Juranic N, Macura S, Botuyan MV, Mer G Biochemistry. 2010 Nov 30;49(47):10198-10207. Epub 2010 Nov 4. PMID:21049971<ref>PMID:21049971</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[DNA polymerase|DNA polymerase]]
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Benirschke, R.]]
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[[Category: Large Structures]]
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[[Category: Cui, G.]]
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[[Category: Benirschke R]]
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[[Category: Mer, G.]]
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[[Category: Cui G]]
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[[Category: Dna polymerase iota]]
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[[Category: Mer G]]
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[[Category: Protein binding]]
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[[Category: Translesion dna synthesis]]
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[[Category: Ubiquitin-binding motif]]
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Current revision

Solution NMR structure of ubiquitin-binding motif (UBM2) of human polymerase iota

PDB ID 2l0g

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