MG_498_MONOMER – formamidopyrimidine-DNA glycosylase

Name
WID MG_498_MONOMER View in model
Name formamidopyrimidine-DNA glycosylase View in model
Cross references PDB: 1K82
 
Genetics
Gene MG_498 View in model
 
Structure
Sequence
1
51
101
151
201
251
MPELPEVTTVINELKETVLNKPLDQVQVNLRKVLKNIDPQLLNKQLKNQF
FTDIKRKGKYIIFLLSNGLYLVSHLRMEGKYFFEERGSKFNQKHVLVEFH
FDDGSQLNYHDTRQFGTFHLYEKLEQAAQLNKLAFDPLEAGFDYRKIFQK
AQNSKRKVKTFILDQTVISGIGNIYADEILFASKINPETMVDQLTIKEIE
ILCKNATKILAKAIVMKGTTISSFSFKKDHTGGYQNFLKVHTKKDQPCSV
CNQLIVKKKINGRGSYFCLNCQKITTKVSTKLNP*
50
100
150
200
250
285
View in model
Is N‑terminal methionine cleaved
Yes
View in model
Prosthetic groups View in model
DNA footprint Length: 9 (nt), Binding: dsDNA, Region: dsDNA View in model
Empirical formula (pH 7.5) H2387C1487N395O418S9
Molecular weight (pH 7.5; Da) 32774.75 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
14035
Instability index 21.84
Is stable True
Aliphatic index 90.60
GRAVY (25C, pH 7.0) -0.380
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Enzyme View in model
Reaction participant View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0074]. Coenzymes Interacts with 1 ZN per monomer as prosthetic group [74]. N-terminal methionine cleavage Shewanella oneidensis MR-1 homolog undergoes N-terminal methionine cleavage [PUB_0280]. DNA-binding Fpg footprint is 9 nt [PUB_0719]. Ogg1 footprint is 10 nt [PUB_0719, PUB_0720, PUB_0721, PUB_0722]. Fpg footprint is 12 nt [PUB_0717].
References
  1. Bruner SD, Norman DP, Verdine GL. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859-66 (2000). WholeCell: PUB_0721, PubMed: 10706276

  2. Castaing B, Boiteux S, Zelwer C. DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase. Nucleic Acids Res 20, 389-94 (1992). WholeCell: PUB_0074, PubMed: 1741272

  3. Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL. Product-assisted catalysis in base-excision DNA repair. Nat Struct Biol 10, 204-11 (2003). WholeCell: PUB_0720, PubMed: 12592398

  4. Gupta N, Tanner S, Jaitly N, Adkins JN, Lipton M, Edwards R, Romine M, Osterman A, Bafna V, Smith RD, Pevzner PA. Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotation. Genome Res 17, 1362-77 (2007). WholeCell: PUB_0280, PubMed: 17690205

  5. Miao F, Bouziane M, O'Connor TR. Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing xsDNA hypoxanthine or abasic sites. Nucleic Acids Res 26, 4034-41 (1998). WholeCell: PUB_0717, PubMed: 9705516

  6. ... 2 more

  7. Norman DP, Bruner SD, Verdine GL. Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein. J Am Chem Soc 123, 359-60 (2001). WholeCell: PUB_0722, PubMed: 11456534

  8. Sidorenko VS, Zharkov DO. Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases. Biochemistry 47, 8970-6 (2008). WholeCell: PUB_0719, PubMed: 18672903

 
Metadata
Created 2012-10-01 15:07:55
Last updated 2012-10-01 15:14:38