| MWexperimental | 71 | kDa |
| MWexpected | 80 | kDa |
| VPorod | 113 | nm3 |
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log I(s)
6.73×10-2
6.73×10-3
6.73×10-4
6.73×10-5
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s, nm-1
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Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.
Kubiak X, Polsinelli I, Chavas LMG, Fyfe CD, Guillot A, Fradale L, Brewee C, Grimaldi S, Gerbaud G, Thureau A, Legrand P, Berteau O, Benjdia A, Nat Chem Biol (2023) Europe PMCSASDRR7 – Radical SAM enzyme peptide epimerase in the presence of SAM (S-adenosyl-L-methionine) and a peptide subtrate
Putative peptide biosynthesis protein YydG|
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Fits and models
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Synchrotron SAXS data from solutions of radical SAM enzyme peptide epimerase with SAM and a peptide subtrate in 25 mM HEPES, 150 mM NaCl, 1 mM DTT, pH 7.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 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 5 mg/ml was injected at a 0.25 ml/min flow rate onto a GE Superdex 200 5/150 column at 20°C. 600 successive 0.990 second frames were collected through the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the SEC-peak sample frames.
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