| MWexperimental | 73 | kDa |
| MWexpected | 77 | kDa |
| VPorod | 145 | nm3 |
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log I(s)
8.46×100
8.46×10-1
8.46×10-2
8.46×10-3
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s, nm-1
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Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes.
Sah-Teli SK, Pinkas M, Hynönen MJ, Butcher SJ, Wierenga RK, Novacek J, Venkatesan R, Structure (2023) Europe PMCSASDKS8 – Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme subunit alpha (anEcTFE-alpha)
Fatty acid oxidation complex subunit alpha|
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Fits and models
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Synchrotron SAXS data from solutions of anEcTFE-alpha in 50 mM Tris, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 4 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 10/300 column at 4°C. 3200 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
This is alpha subunit of E. coli anaerobic fatty acid beta oxidation trifunctional enzyme (anEcTFE) complex. It catalyzes the second and third step of fatty acid beta oxidation beta oxidation cycle in E. coli under anaerobic conditions. It is encoded by fadJ gene. |
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