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5ITY

Crystal Structure of Human NEIL1(P2G) bound to duplex DNA containing Thymine Glycol

Summary for 5ITY
Entry DOI10.2210/pdb5ity/pdb
Related5ITQ 5ITR 5ITT 5ITU 5ITX
DescriptorEndonuclease 8-like 1, DNA (26-MER), GLYCEROL, ... (4 entities in total)
Functional Keywordsdna glycosylase neil1 fpg nei base excision repair, dna binding protein-dna complex, dna binding protein/dna
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm, cytoskeleton, microtubule organizing center, centrosome : Q96FI4
Total number of polymer chains6
Total formula weight158742.45
Authors
Zhu, C.,Lu, L.,Zhang, J.,Yue, Z.,Song, J.,Zong, S.,Liu, M.,Stovicek, O.,Gao, Y.,Yi, C. (deposition date: 2016-03-17, release date: 2016-07-06, Last modification date: 2023-11-08)
Primary citationZhu, 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: 27354518
DOI: 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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数据于2024-10-30公开中

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