MG_244_DIMER – 3-5' helicase

Name
WID MG_244_DIMER View in model
Name 3-5' helicase View in model
 
Structure
Biosynthesis [c]: (2) MG_244_MONOMERMG_244_DIMER View in model
No. subunits 2
DNA footprint Length: 15 (nt), Binding: dsDNA, Region: dsDNA View in model
Empirical formula (pH 7.5) H11794C7462N1922O2164S28
Molecular weight (pH 7.5; Da) 163952.42 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
-154810.00
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200.00 View in model
 
Synthesis
Formation process Process_MacromolecularComplexation View in model
Localization c
 
Function
Enzyme DNA excision
[c]: ATP + H2OADP + H + PI
View in model
Reaction participant View in model
Complex subunit 3-5' helicase
[c]: (2) MG_244_MONOMERMG_244_DIMER
View in model
 
Parameters
Parameters Parameter_0054: NER_PcrA_StepSize = 1 b View in model
 
Comments
Comments Composition [PUB_0077]. DNA-binding Step size is 1 bp [PUB_0516]. Exonuclease III footprint is 15 nt [PUB_0714]. PriA footprinti is 28 nt [PUB_0715].
References
  1. Maluf NK, Fischer CJ, Lohman TM. A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J Mol Biol 325, 913-35 (2003). WholeCell: PUB_0077, PubMed: 12527299

  2. Marians KJ. PriA: at the crossroads of DNA replication and recombination. Prog Nucleic Acid Res Mol Biol 63, 39-67 (1999). WholeCell: PUB_0715, PubMed: 10506828

  3. Park J, Myong S, Niedziela-Majka A, Lee KS, Yu J, Lohman TM, Ha T. PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps. Cell 142, 544-55 (2010). WholeCell: PUB_0714, PubMed: 20723756

  4. Tomko EJ, Fischer CJ, Niedziela-Majka A, Lohman TM. A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol Cell 26, 335-47 (2007). WholeCell: PUB_0516, PubMed: 17499041

 
Metadata
Created 2012-10-01 15:07:39
Last updated 2012-10-01 15:14:10