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- H2TH_domain abstract "In molecular biology, the H2TH domain (helix-2turn-helix domain) is a DNA-binding domain found in DNA glycosylase/AP lyase enzymes, which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Most damage to bases in DNA is repaired by the base excision repair pathway. These enzymes are primarily from bacteria, and have both DNA glycosylase activity EC 3.2.2.- and AP lyase activity EC 4.2.99.18. Examples include formamidopyrimidine-DNA glycosylases (Fpg; MutM) and endonuclease VIII (Nei).Formamidopyrimidine-DNA glycosylases (Fpg, MutM) is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidation-damaged bases (N-glycosylase activity; EC 3.2.2.23) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity;EC 4.2.99.18). Fpg has a preference for oxidised purines, excising oxidised purine bases such as 7,8-dihydro-8-oxoguanine (8-oxoG). Its AP (apurinic/apyrimidinic) lyase activity introduces nicks in the DNA strand, cleaving the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Fpg is a monomer composed of 2 domains connected by a flexible hinge. The two DNA-binding motifs (a zinc finger and the H2TH (helix-two-turns-helix) motifs) suggest that the oxidised base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes. Fpg binds one ion of zinc at the C terminus, which contains four conserved and essential cysteines.Endonuclease VIII (Nei) has the same enzyme activities as Fpg above (EC 3.2.2.-,EC 4.2.99.18), but with a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. These proteins contain three structural domains: an N-terminal catalytic core domain, a central helix-two turn-helix (H2TH) module and a C-terminal zinc finger (see PDB:1K82). The N-terminal catalytic domain and the C-terminal zinc finger straddle the DNA with the long axis of the protein oriented roughly orthogonal to the helical axis of the DNA. Residues that contact DNA are located in the catalytic domain and in a beta-hairpin loop formed by the zinc finger.".
- H2TH_domain symbol "H2TH".
- H2TH_domain thumbnail PDB_1tdz_EBI.jpg?width=300.
- H2TH_domain wikiPageID "33376060".
- H2TH_domain wikiPageLength "5913".
- H2TH_domain wikiPageOutDegree "41".
- H2TH_domain wikiPageRevisionID "607880282".
- H2TH_domain wikiPageWikiLink Base_excision_repair.
- H2TH_domain wikiPageWikiLink Base_pair.
- H2TH_domain wikiPageWikiLink Biocatalysis.
- H2TH_domain wikiPageWikiLink Biomolecular_structure.
- H2TH_domain wikiPageWikiLink Bond_cleavage.
- H2TH_domain wikiPageWikiLink Catalysis.
- H2TH_domain wikiPageWikiLink Category:Protein_domains.
- H2TH_domain wikiPageWikiLink Conserved_sequence.
- H2TH_domain wikiPageWikiLink Cysteine.
- H2TH_domain wikiPageWikiLink DNA.
- H2TH_domain wikiPageWikiLink DNA-(apurinic_or_apyrimidinic_site)_lyase.
- H2TH_domain wikiPageWikiLink DNA_glycosylase.
- H2TH_domain wikiPageWikiLink DNA_repair.
- H2TH_domain wikiPageWikiLink Dihydrothymine.
- H2TH_domain wikiPageWikiLink Dihydrouracil.
- H2TH_domain wikiPageWikiLink Endonuclease.
- H2TH_domain wikiPageWikiLink Enzyme.
- H2TH_domain wikiPageWikiLink Helix.
- H2TH_domain wikiPageWikiLink Ion.
- H2TH_domain wikiPageWikiLink Molecular_binding.
- H2TH_domain wikiPageWikiLink Monomer.
- H2TH_domain wikiPageWikiLink Mutagen.
- H2TH_domain wikiPageWikiLink Nucleotide.
- H2TH_domain wikiPageWikiLink Phosphate.
- H2TH_domain wikiPageWikiLink Phosphodiester_bond.
- H2TH_domain wikiPageWikiLink Protein.
- H2TH_domain wikiPageWikiLink Protein_domain.
- H2TH_domain wikiPageWikiLink Purine.
- H2TH_domain wikiPageWikiLink Pyrimidine.
- H2TH_domain wikiPageWikiLink Redox.
- H2TH_domain wikiPageWikiLink Residue_(chemistry).
- H2TH_domain wikiPageWikiLink Structural_motif.
- H2TH_domain wikiPageWikiLink Turn_(biochemistry).
- H2TH_domain wikiPageWikiLink Zinc.
- H2TH_domain wikiPageWikiLink Zinc_finger.
- H2TH_domain wikiPageWikiLinkText "H2TH domain".
- H2TH_domain caption "crystal structure complex between the lactococcus lactis fpg and a fapy-dg containing dna".
- H2TH_domain interpro "IPR015886".
- H2TH_domain name "H2TH".
- H2TH_domain pfam "PF06831".
- H2TH_domain pfamClan "CL0303".
- H2TH_domain prosite "PDOC00956".
- H2TH_domain scop "1".
- H2TH_domain symbol "H2TH".
- H2TH_domain wikiPageUsesTemplate Template:EC_number.
- H2TH_domain wikiPageUsesTemplate Template:Infobox_protein_family.
- H2TH_domain wikiPageUsesTemplate Template:InterPro_content.
- H2TH_domain wikiPageUsesTemplate Template:Reflist.
- H2TH_domain subject Category:Protein_domains.
- H2TH_domain hypernym Domain.
- H2TH_domain type Biomolecule.
- H2TH_domain type Protein.
- H2TH_domain type Chemical.
- H2TH_domain type Domain.
- H2TH_domain type Thing.
- H2TH_domain type Q206229.
- H2TH_domain type Q8054.
- H2TH_domain comment "In molecular biology, the H2TH domain (helix-2turn-helix domain) is a DNA-binding domain found in DNA glycosylase/AP lyase enzymes, which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Most damage to bases in DNA is repaired by the base excision repair pathway. These enzymes are primarily from bacteria, and have both DNA glycosylase activity EC 3.2.2.- and AP lyase activity EC 4.2.99.18.".
- H2TH_domain label "H2TH domain".
- H2TH_domain sameAs Q5628836.
- H2TH_domain sameAs m.0h97zzj.
- H2TH_domain sameAs Q5628836.
- H2TH_domain wasDerivedFrom H2TH_domain?oldid=607880282.
- H2TH_domain depiction PDB_1tdz_EBI.jpg.
- H2TH_domain isPrimaryTopicOf H2TH_domain.