Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes.

Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R, Biochem J (2019) Europe PMC

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex

anaerobic Fatty acid oxidation complex subunit alpha
anaerobic Fatty acid oxidation complex subunit alpha
anaerobic Fatty acid oxidation complex subunit alpha
anaerobic Fatty acid oxidation complex subunit alpha
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit
MWexperimental 535 kDa
MWexpected 501 kDa
VPorod 856 nm3
log I(s) 5.89×101 5.89×100 5.89×10-1 5.89×10-2
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit small angle scattering data  s, nm-1
ln I(s)
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit Guinier plot ln 5.89×101 Rg: 6.2 nm 0 (6.2 nm)-2 s2
(sRg)2I(s)/I(0)
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit Kratky plot 1.104 0 3 sRg
p(r)
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit pair distance distribution function Rg: 6.2 nm 0 Dmax: 19.6 nm

Data validation


Fits and models


log I(s)
 s, nm-1
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit DAMMIN model

log I(s)
 s, nm-1
anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic Fatty acid oxidation complex subunit alpha anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit SWISSMODEL model

Synchrotron SAXS data from solutions of anEcTFE in 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH 8 were measured at 20°C using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The data were collected as 1200 successive 1 second frames through the SEC elution profile (sample concentration = 3.5 mg/ml ). The SAXS data were measured from the sample and buffer from a Superdex 200 5/150 GL, (GE Healthcare) column at flow rate of 0.16 mL/min. The sample-peak data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.

anaerobic Fatty acid oxidation complex subunit alpha (anEcTFE-alpha)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   77.1 kDa
 
UniProt   P77399
Sequence   FASTA
 
anaerobic Fatty acid oxidation complex subunit alpha (anEcTFE-alpha)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   77.1 kDa
 
UniProt   P77399
Sequence   FASTA
 
anaerobic Fatty acid oxidation complex subunit alpha (anEcTFE-alpha)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   77.1 kDa
 
UniProt   P77399
Sequence   FASTA
 
anaerobic Fatty acid oxidation complex subunit alpha (anEcTFE-alpha)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   77.1 kDa
 
UniProt   P77399
Sequence   FASTA
 
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit (anEcTFE-beta)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   48.1 kDa
 
UniProt   P76503
Sequence   FASTA
 
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit (anEcTFE-beta)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   48.1 kDa
 
UniProt   P76503
Sequence   FASTA