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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== |
| <StructureSection load='2l0g' size='340' side='right' caption='[[2l0g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2l0g' size='340' side='right'caption='[[2l0g]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2l0g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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> | | <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> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l0f|2l0f]]</td></tr> | | </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'>[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://pdbe.org/2l0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l0g RCSB], [http://www.ebi.ac.uk/pdbsum/2l0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0g 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=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> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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> | | [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> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2l0g" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[DNA polymerase|DNA polymerase]] | | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Benirschke, R]] | | [[Category: Large Structures]] |
| [[Category: Cui, G]] | | [[Category: Benirschke R]] |
| [[Category: Mer, G]] | | [[Category: Cui G]] |
| [[Category: Dna polymerase iota]] | | [[Category: Mer G]] |
| [[Category: Protein binding]]
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| [[Category: Translesion dna synthesis]]
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| [[Category: Ubiquitin-binding motif]]
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