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- FPG_IleRS_zinc_finger abstract "The FPG IleRS zinc finger domain represents a zinc finger domain found at the C-terminal in both DNA glycosylase/AP lyase enzymes and in isoleucyl tRNA synthetase. In these two types of enzymes, the C-terminal domain forms a zinc finger.DNA glycosylase/AP lyase enzymes are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. These enzymes have both DNA glycosylase activity (EC) and AP lyase activity (EC). 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) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity; EC). Fpg has a preference for oxidised purines, excising oxidized 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 helix-two-turns-helix motifs) suggest that the oxidized 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, but with a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine.An Fpg-type zinc finger is also found at the C terminus of isoleucyl tRNA synthetase (EC). This enzyme catalyses the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pre-transfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'post-transfer' editing and involves deacylation of mischarged Val-tRNA(Ile).".
- FPG_IleRS_zinc_finger symbol "zf-FPG_IleRS".
- FPG_IleRS_zinc_finger thumbnail PDB_1tdz_EBI.jpg?width=300.
- FPG_IleRS_zinc_finger wikiPageExternalLink 3.2.2.
- FPG_IleRS_zinc_finger wikiPageExternalLink 3.2.2.23.
- FPG_IleRS_zinc_finger wikiPageExternalLink 4.2.99.18.
- FPG_IleRS_zinc_finger wikiPageExternalLink 6.1.1.5.
- FPG_IleRS_zinc_finger wikiPageID "31997273".
- FPG_IleRS_zinc_finger wikiPageLength "6781".
- FPG_IleRS_zinc_finger wikiPageOutDegree "26".
- FPG_IleRS_zinc_finger wikiPageRevisionID "591356274".
- FPG_IleRS_zinc_finger wikiPageWikiLink Amino_acid.
- FPG_IleRS_zinc_finger wikiPageWikiLink Base_(chemistry).
- FPG_IleRS_zinc_finger wikiPageWikiLink Base_excision_repair.
- FPG_IleRS_zinc_finger wikiPageWikiLink Bond_cleavage.
- FPG_IleRS_zinc_finger wikiPageWikiLink Catalysis.
- FPG_IleRS_zinc_finger wikiPageWikiLink Category:Protein_domains.
- FPG_IleRS_zinc_finger wikiPageWikiLink Chemical_bond.
- FPG_IleRS_zinc_finger wikiPageWikiLink Conserved_sequence.
- FPG_IleRS_zinc_finger wikiPageWikiLink Cysteine.
- FPG_IleRS_zinc_finger wikiPageWikiLink Endonuclease.
- FPG_IleRS_zinc_finger wikiPageWikiLink Enzyme.
- FPG_IleRS_zinc_finger wikiPageWikiLink Enzymes.
- FPG_IleRS_zinc_finger wikiPageWikiLink Hydrolysis.
- FPG_IleRS_zinc_finger wikiPageWikiLink Ion.
- FPG_IleRS_zinc_finger wikiPageWikiLink Isoleucine.
- FPG_IleRS_zinc_finger wikiPageWikiLink Ligase.
- FPG_IleRS_zinc_finger wikiPageWikiLink Monomer.
- FPG_IleRS_zinc_finger wikiPageWikiLink Nucleotide.
- FPG_IleRS_zinc_finger wikiPageWikiLink Oxidation.
- FPG_IleRS_zinc_finger wikiPageWikiLink Purine.
- FPG_IleRS_zinc_finger wikiPageWikiLink Redox.
- FPG_IleRS_zinc_finger wikiPageWikiLink Structurally.
- FPG_IleRS_zinc_finger wikiPageWikiLink Structure.
- FPG_IleRS_zinc_finger wikiPageWikiLink Synthetase.
- FPG_IleRS_zinc_finger wikiPageWikiLink Virus.
- FPG_IleRS_zinc_finger wikiPageWikiLink Zinc_finger.
- FPG_IleRS_zinc_finger caption "Crystal structure complex between the lactococcus lactis fpg and a fapy-dg containing DNA".
- FPG_IleRS_zinc_finger hasPhotoCollection FPG_IleRS_zinc_finger.
- FPG_IleRS_zinc_finger interpro "IPR010663".
- FPG_IleRS_zinc_finger name "zf-FPG_IleRS".
- FPG_IleRS_zinc_finger pfam "PF06827".
- FPG_IleRS_zinc_finger pfamClan "CL0167".
- FPG_IleRS_zinc_finger scop "1".
- FPG_IleRS_zinc_finger symbol "zf-FPG_IleRS".
- FPG_IleRS_zinc_finger wikiPageUsesTemplate Template:Infobox_protein_family.
- FPG_IleRS_zinc_finger wikiPageUsesTemplate Template:Reflist.
- FPG_IleRS_zinc_finger subject Category:Protein_domains.
- FPG_IleRS_zinc_finger type Biomolecule.
- FPG_IleRS_zinc_finger type Protein.
- FPG_IleRS_zinc_finger type Chemical.
- FPG_IleRS_zinc_finger type Domain.
- FPG_IleRS_zinc_finger type Thing.
- FPG_IleRS_zinc_finger type Q206229.
- FPG_IleRS_zinc_finger type Q8054.
- FPG_IleRS_zinc_finger comment "The FPG IleRS zinc finger domain represents a zinc finger domain found at the C-terminal in both DNA glycosylase/AP lyase enzymes and in isoleucyl tRNA synthetase. In these two types of enzymes, the C-terminal domain forms a zinc finger.DNA glycosylase/AP lyase enzymes are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. These enzymes have both DNA glycosylase activity (EC) and AP lyase activity (EC).".
- FPG_IleRS_zinc_finger label "FPG IleRS zinc finger".
- FPG_IleRS_zinc_finger sameAs m.0gvsvbc.
- FPG_IleRS_zinc_finger sameAs Q5426994.
- FPG_IleRS_zinc_finger sameAs Q5426994.
- FPG_IleRS_zinc_finger wasDerivedFrom FPG_IleRS_zinc_finger?oldid=591356274.
- FPG_IleRS_zinc_finger depiction PDB_1tdz_EBI.jpg.
- FPG_IleRS_zinc_finger isPrimaryTopicOf FPG_IleRS_zinc_finger.