Crystal structure of the phospholipase A and acyltransferase 4 (PLAAT4) catalytic domain.

Wehlin A, Cornaciu I, Marquez JA, Perrakis A, von Castelmur E, J Struct Biol 214(4):107903 (2022) Europe PMC

SASDQN6 – The N-terminal domain of Phospholipase A and acyltransferase 4 (PLAAT4 NTD)

Phospholipase A and acyltransferase 4
MWexperimental 16 kDa
MWexpected 14 kDa
VPorod 31 nm3
log I(s) 2.53×10-2 2.53×10-3 2.53×10-4 2.53×10-5
Phospholipase A and acyltransferase 4 small angle scattering data  s, nm-1
ln I(s)
Phospholipase A and acyltransferase 4 Guinier plot ln 2.54×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Phospholipase A and acyltransferase 4 Kratky plot 1.104 0 √3 sRg
p(r)
Phospholipase A and acyltransferase 4 pair distance distribution function Rg: 1.9 nm 0 Dmax: 7.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Phospholipase A and acyltransferase 4 PYMOL model
log I(s)
 s, nm-1
Phospholipase A and acyltransferase 4 SREFLEX model
Synchrotron SAXS data from solutions of the N-terminal domain of PLAAT4 in 20 mM HEPES pH 7.4, 150 mM NaCl, 2 mM TECP, 1% glycerol, were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.155 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 40 μl sample at 12.6 mg/ml was injected at a 0.35 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 20°C. 2880 successive 0.25 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.

Phospholipase A and acyltransferase 4 (PLAAT4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   14.0 kDa
 
UniProt   Q9UL19 (1-123)
Sequence   FASTA