Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition.

Anandan A, Dunstan NW, Ryan TM, Mertens HDT, Lim KYL, Evans GL, Kahler CM, Vrielink A, IUCrJ 8(Pt 5):732-746 (2021) Europe PMC

SASDK38 – Lipid A phosphoethanolamine transferase in n-dodecyl-β-D maltoside micelles

YhbX/YhjW/YijP/YjdB family protein (L152F)
MWexperimental 200 kDa
MWexpected 62 kDa
VPorod 304 nm3
log I(s) 1.32×10-2 1.32×10-3 1.32×10-4 1.32×10-5
YhbX/YhjW/YijP/YjdB family protein (L152F) small angle scattering data  s, nm-1
ln I(s)
YhbX/YhjW/YijP/YjdB family protein (L152F) Guinier plot ln 1.32×10-2 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
YhbX/YhjW/YijP/YjdB family protein (L152F) Kratky plot 1.104 0 √3 sRg
p(r)
YhbX/YhjW/YijP/YjdB family protein (L152F) pair distance distribution function Rg: 4.2 nm 0 Dmax: 12.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Lipid A phosphoethanolamine transferase in n-dodecyl-β-D maltoside micelles Rg histogram Rg, nm
log I(s)
 s, nm-1
YhbX/YhjW/YijP/YjdB family protein (L152F) MEMPROT model
log I(s)
 s, nm-1
YhbX/YhjW/YijP/YjdB family protein (L152F) OTHER model
Synchrotron SAXS data from solutions of Lipid A phosphoethanolamine transferase in 50 mM HEPES, 100 mM NaCl, 0.023% n-Dodecyl β-D-maltoside (DDM), pH 7 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 1.5 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 7 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN. Number of frames = UNKNOWN

YhbX/YhjW/YijP/YjdB family protein (L152F) (EptA (L152F))
Mol. type   Protein
Organism   Neisseria meningitidis serogroup B (strain MC58)
Olig. state   Monomer
Mon. MW   62.2 kDa
 
UniProt   Q7DD94 (1-544)
Sequence   FASTA
 
PDB ID   5FGN
 
PDB ID   5FGN