Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.

Sajko S, Grishkovskaya I, Kostan J, Graewert M Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K, PLoS One 15(12):e0242677 (2020) Europe PMC

SASDGC7 – Plasmodium falciparum Membrane Occupation and Recognition Nexus (MORN1) repeats 7-15

MORN repeat-containing protein 1
MWI(0) 52 kDa
MWexpected 46 kDa
VPorod 52 nm3
log I(s) 5.80×10-2 5.80×10-3 5.80×10-4 5.80×10-5
MORN repeat-containing protein 1 small angle scattering data  s, nm-1
ln I(s)
MORN repeat-containing protein 1 Guinier plot ln 5.80×10-2 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
MORN repeat-containing protein 1 Kratky plot 1.104 0 √3 sRg
p(r)
MORN repeat-containing protein 1 pair distance distribution function Rg: 4.2 nm 0 Dmax: 16 nm

Data validation

Fits and models

log I(s)
 s, nm-1
MORN repeat-containing protein 1 DAMMIN model
log I(s)
 s, nm-1
MORN repeat-containing protein 1 CUSTOM IN-HOUSE model
Synchrotron SAXS data from solutions of Plasmodium falciparum Membrane Occupation and Recognition Nexus (MORN1) repeats 7-15 in 20 mM Tris-HCl, 100 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 10°C. 20 successive 0.050 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.

MORN repeat-containing protein 1 (pf MORN1 delta 6)
Mol. type   Protein
Organism   Plasmodium falciparum
Olig. state   Dimer
Mon. MW   23.1 kDa
 
UniProt   Q8IJ93 (162-364)
Sequence   FASTA