5itq

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==Crystal Structure of Human NEIL1, Free Protein==
==Crystal Structure of Human NEIL1, Free Protein==
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<StructureSection load='5itq' size='340' side='right' caption='[[5itq]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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<StructureSection load='5itq' size='340' side='right'caption='[[5itq]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5itq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5itq]] is a 1 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=5ITQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ITQ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itx|5itx]], [[5ity|5ity]], [[5itt|5itt]], [[5itu|5itu]]</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">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</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=5itq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itq OCA], [http://pdbe.org/5itq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itq RCSB], [http://www.ebi.ac.uk/pdbsum/5itq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itq ProSAT]</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=5itq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itq OCA], [https://pdbe.org/5itq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5itq RCSB], [https://www.ebi.ac.uk/pdbsum/5itq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5itq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NEIL1_HUMAN NEIL1_HUMAN]] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches.<ref>PMID:12200441</ref> <ref>PMID:12509226</ref> <ref>PMID:11904416</ref> <ref>PMID:14522990</ref>
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[https://www.uniprot.org/uniprot/NEIL1_HUMAN NEIL1_HUMAN] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches.<ref>PMID:12200441</ref> <ref>PMID:12509226</ref> <ref>PMID:11904416</ref> <ref>PMID:14522990</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NEIL1 (Nei-like 1) is a DNA repair glycosylase guarding the mammalian genome against oxidized DNA bases. As the first enzymes in the base-excision repair pathway, glycosylases must recognize the cognate substrates and catalyze their excision. Here we present crystal structures of human NEIL1 bound to a range of duplex DNA. Together with computational and biochemical analyses, our results suggest that NEIL1 promotes tautomerization of thymine glycol (Tg)-a preferred substrate-for optimal binding in its active site. Moreover, this tautomerization event also facilitates NEIL1-catalyzed Tg excision. To our knowledge, the present example represents the first documented case of enzyme-promoted tautomerization for efficient substrate recognition and catalysis in an enzyme-catalyzed reaction.
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Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.,Zhu C, Lu L, Zhang J, Yue Z, Song J, Zong S, Liu M, Stovicek O, Gao YQ, Yi C Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):7792-7. doi:, 10.1073/pnas.1604591113. Epub 2016 Jun 27. PMID:27354518<ref>PMID:27354518</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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<div class="pdbe-citations 5itq" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gao, Y]]
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[[Category: Homo sapiens]]
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[[Category: Liu, M]]
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[[Category: Large Structures]]
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[[Category: Lu, L]]
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[[Category: Gao Y]]
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[[Category: Song, J]]
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[[Category: Liu M]]
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[[Category: Stovicek, O]]
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[[Category: Lu L]]
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[[Category: Yi, C]]
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[[Category: Song J]]
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[[Category: Yue, Z]]
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[[Category: Stovicek O]]
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[[Category: Zhang, J]]
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[[Category: Yi C]]
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[[Category: Zhu, C]]
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[[Category: Yue Z]]
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[[Category: Zong, S]]
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[[Category: Zhang J]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Zhu C]]
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[[Category: Dna glycosylase neil1 fpg nei base excision repair]]
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[[Category: Zong S]]

Current revision

Crystal Structure of Human NEIL1, Free Protein

PDB ID 5itq

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