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