A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase.

Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G, J Mol Biol 392(2):334-51 (2009) Europe PMC

SASDAQ4 – 6:3 complex of GAD:CaM

Calmodulin
Glutamate decarboxylase
MWexperimental 400 kDa
MWexpected 357 kDa
VPorod 630 nm3
log I(s) 8.76×104 8.76×103 8.76×102 8.76×101
Calmodulin Glutamate decarboxylase small angle scattering data  s, nm-1
ln I(s)
Calmodulin Glutamate decarboxylase Guinier plot ln 8.76×104 Rg: 5.9 nm 0 (5.9 nm)-2 s2
(sRg)2I(s)/I(0)
Calmodulin Glutamate decarboxylase Kratky plot 1.104 0 √3 sRg
p(r)
Calmodulin Glutamate decarboxylase pair distance distribution function 0 Dmax: 23 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Calmodulin Glutamate decarboxylase BUNCH model
Synchrotron SAXS data from solutions of 6:3 complex of GAD:CaM in 50 mM HEPES 50 mM KCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). . The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN

Tags: X33
Calmodulin
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   16.8 kDa
 
UniProt   P62158
Sequence   FASTA
 
Glutamate decarboxylase (GAD)
Mol. type   Protein
Organism   Petunia x hybrida
Olig. state   Hexamer
Mon. MW   56.7 kDa
 
UniProt   Q07346
Sequence   FASTA