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4JGC

Human TDG N140A mutant IN A COMPLEX WITH 5-carboxylcytosine (5caC)

Summary for 4JGC
Entry DOI10.2210/pdb4jgc/pdb
Related4FNC
DescriptorG/T mismatch-specific thymine DNA glycosylase, oligonucleotide, oligonucleotide containing 5-carboxylcytosine, ... (5 entities in total)
Functional Keywords5-carboxylcytosine; thymine dna glycosylase; dna modification; dna 5mc oxidation; epigenetic regulation, dna demethylation, 5-carboxylcytosine, hydrolase-dna complex, hydrolase/dna
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q13569
Total number of polymer chains3
Total formula weight40302.75
Authors
Hashimoto, H.,Zhang, X.,Cheng, X. (deposition date: 2013-02-28, release date: 2013-05-29, Last modification date: 2023-09-20)
Primary citationHashimoto, H.,Zhang, X.,Cheng, X.
Activity and crystal structure of human thymine DNA glycosylase mutant N140A with 5-carboxylcytosine DNA at low pH.
Dna Repair, 12:535-540, 2013
Cited by
PubMed Abstract: The mammalian thymine DNA glycosylase (TDG) excises 5-carboxylcytosine (5caC) when paired with a guanine in a CpG sequence, in addition to mismatched bases. Here we present a complex structure of the human TDG catalytic mutant, asparagine 140 to alanine (N140A), with a 28-base pair DNA containing a G:5caC pair at pH 4.6. TDG interacts with the carboxylate moiety of target nucleotide 5caC using the side chain of asparagine 230 (N230), instead of asparagine 157 (N157) as previously reported. Mutation of either N157 or N230 residues to aspartate has minimal effect on G:5caC activity while significantly reducing activity on G:U substrate. Combination of both the asparagine-to-aspartate mutations (N157D/N230D) resulted in complete loss of activity on G:5caC while retaining measurable activity on G:U, implying that 5caC can adopt alternative conformations (either N157-interacting or N230-interacting) in the TDG active site to interact with either of the two asparagine side chain for 5caC excision.
PubMed: 23680598
DOI: 10.1016/j.dnarep.2013.04.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.582 Å)
Structure validation

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