1kea

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STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASESTRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE

Structural highlights

1kea is a 1 chain structure with sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MIG_METTF DNA glycosylase that excises thymine from T/G mismatches and uracil from U/G mismatches (PubMed:8895589, PubMed:11788726). Acts as a repair enzyme able to counteract the mutagenic effect of spontaneous hydrolytic deamination of DNA 5-methylcytosine (5-meC) residues that leads to the formation of T/G mismatches (PubMed:8895589). May also repair U/G mismatches arising from hydrolytic deamination of DNA cytosine residues (PubMed:8895589). G/G, A/G, T/C and U/C are minor substrates (PubMed:8895589, PubMed:11788726).[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Fondufe-Mittendorf YN, Härer C, Kramer W, Fritz HJ. Two amino acid replacements change the substrate preference of DNA mismatch glycosylase Mig.MthI from T/G to A/G. Nucleic Acids Res. 2002 Jan 15;30(2):614-21. PMID:11788726 doi:10.1093/nar/30.2.614
  2. Horst JP, Fritz HJ. Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig.Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF. EMBO J. 1996 Oct 1;15(19):5459-69 PMID:8895589

1kea, resolution 2.00Å

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OCA