MG_106_MONOMER – peptide deformylase

Name
WID MG_106_MONOMER View in model
Name peptide deformylase View in model
Cross references PDB: 1LRU, PDB: 2DTF
 
Genetics
Gene MG_106 View in model
 
Structure
Sequence
1
51
101
151
MTFQPTKTWLVFDDNALINKPTEAVNFPIDEQIETCIKKMIAYVDASYDG
KAQEYDIIPGIGIAANQIGYWKQLFYIHLNDLNKEKKCLLINPKIIDQSE
NKAFLESGEGCLSVKKQHKGYVIRSEWITIKGYDWFEKKEITIKATGLFG
MCLQHEFDHLQGRFFYQRINPLNPWFKKPEWKVINPTLKTSNG*
50
100
150
194
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H1584C1036N260O286S7
Molecular weight (pH 7.5; Da) 22481.62 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
45420
Instability index 36.80
Is stable True
Aliphatic index 83.97
GRAVY (25C, pH 7.0) -0.416
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Complex subunit peptide deformylase
[c]: (2) MG_106_MONOMERMG_106_DIMER
View in model
 
Comments
Comments Functional Macromolecule Functional as homodimer [PUB_0326, PUB_0327]. Coenzymes Interacts with 1 FE2, NI or CO per monomer as prosthetic group [22,96,386,387].
References
  1. Zhou Z, Song X, Gong W. Novel conformational states of peptide deformylase from pathogenic bacterium Leptospira interrogans: implications for population shift. J Biol Chem 280, 42391-6 (2005). WholeCell: PUB_0326, PubMed: 16239225

  2. Zhou Z, Song X, Li Y, Gong W. Unique structural characteristics of peptide deformylase from pathogenic bacterium Leptospira interrogans. J Mol Biol 339, 207-15 (2004). WholeCell: PUB_0327, PubMed: 15123432

 
Metadata
Created 2012-10-01 15:07:48
Last updated 2012-10-01 15:14:27