3UO7

Crystal structure of Human Thymine DNA Glycosylase Bound to Substrate 5-carboxylcytosine


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA.

Zhang, L.Lu, X.Lu, J.Liang, H.Dai, Q.Xu, G.L.Luo, C.Jiang, H.He, C.

(2012) Nat Chem Biol 8: 328-330

  • DOI: https://doi.org/10.1038/nchembio.914
  • Primary Citation of Related Structures:  
    3UO7, 3UOB

  • PubMed Abstract: 

    Human thymine DNA glycosylase (hTDG) efficiently excises 5-carboxylcytosine (5caC), a key oxidation product of 5-methylcytosine in genomic DNA, in a recently discovered cytosine demethylation pathway. We present here the crystal structures of the hTDG catalytic domain in complex with duplex DNA containing either 5caC or a fluorinated analog. These structures, together with biochemical and computational analyses, reveal that 5caC is specifically recognized in the active site of hTDG, supporting the role of TDG in mammalian 5-methylcytosine demethylation.


  • Organizational Affiliation

    Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
G/T mismatch-specific thymine DNA glycosylaseC [auth A],
D [auth B]
201Homo sapiensMutation(s): 1 
Gene Names: TDG
EC: 3.2.2.29
UniProt & NIH Common Fund Data Resources
Find proteins for Q13569 (Homo sapiens)
Explore Q13569 
Go to UniProtKB:  Q13569
PHAROS:  Q13569
GTEx:  ENSG00000139372 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13569
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-D(*CP*AP*GP*CP*TP*CP*TP*GP*TP*AP*CP*AP*TP*GP*AP*GP*CP*AP*GP*TP*GP*GP*A)-3'A [auth C]23N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(1CC)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3'B [auth D]23N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.232 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 164.352α = 90
b = 164.352β = 90
c = 57.569γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASESphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-02-15
    Type: Initial release
  • Version 1.1: 2015-06-03
    Changes: Database references
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Derived calculations, Refinement description