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 Jun 25)

PMID: 31235482 doi: 10.1042/BCJ20190314

Submitted to SASBDB: 2018 Dec 28 Published in SASBDB: 2019 Jul 2

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein 3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2 Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30 RgGuinier 4.6 nm Dmax 16.0 nm VolumePorod 406 nm3

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH: 8 Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 22 RgGuinier 6.2 nm Dmax 19.6 nm VolumePorod 856 nm3