5ITY
Crystal Structure of Human NEIL1(P2G) bound to duplex DNA containing Thymine Glycol
Summary for 5ITY
Entry DOI | 10.2210/pdb5ity/pdb |
Related | 5ITQ 5ITR 5ITT 5ITU 5ITX |
Descriptor | Endonuclease 8-like 1, DNA (26-MER), GLYCEROL, ... (4 entities in total) |
Functional Keywords | dna glycosylase neil1 fpg nei base excision repair, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Homo sapiens (Human) More |
Cellular location | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : Q96FI4 |
Total number of polymer chains | 6 |
Total formula weight | 158742.45 |
Authors | |
Primary citation | Zhu, C.,Lu, L.,Zhang, J.,Yue, Z.,Song, J.,Zong, S.,Liu, M.,Stovicek, O.,Gao, Y.Q.,Yi, C. Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair Proc.Natl.Acad.Sci.USA, 113:7792-7797, 2016 Cited by PubMed Abstract: 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. PubMed: 27354518DOI: 10.1073/pnas.1604591113 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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