MG_289_290_291_PENTAMER – phosphonate ABC transporter

Name
WID MG_289_290_291_PENTAMER View in model
Name phosphonate ABC transporter View in model
 
Structure
Biosynthesis MG_289_MONOMER[e] + (2) MG_290_MONOMER[c] + (2) MG_291_MONOMER[m] ⇒ MG_289_290_291_PENTAMER[m] View in model
No. subunits 5
Empirical formula (pH 7.5) H16534C10586N2534O2765S30
Molecular weight (pH 7.5; Da) 224503.16 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
-284195.00
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 m
 
Function
Enzyme 2-aminoethylphosphonate transport via ABC system
AEPP[e] + ATP[c] + H2O[c] ⇒ ADP[c] + AEPP[c] + H[c] + PI[c]
View in model
Complex subunit phosphonate ABC transporter
MG_289_MONOMER[e] + (2) MG_290_MONOMER[c] + (2) MG_291_MONOMER[m] ⇒ MG_289_290_291_PENTAMER[m]
View in model
 
Comments
Comments Sippel et al suggest that MG_289, the substrate-binding subunit of this ABC transporter, has a thiamine binding domain, suggesting that MG_289 may be responsive to thiamine and other substrates beyond phosphonate [PUB_0798].
References
  1. Sippel KH, Venkatakrishnan B, Boehlein SK, Sankaran B, Quirit JG, Govindasamy L, Agbandje-McKenna M, Goodison S, Rosser CJ, McKenna R. Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein. Proteins 79, 528-36 (2011). WholeCell: PUB_0798, PubMed: 21117240

 
Metadata
Created 2012-10-01 15:07:40
Last updated 2012-10-01 15:14:12