Glutamate decarboxylase (Gad) catalyzes glutamate to γ-aminobutyrateconversion. Plant Gad is a ∼340 kDa hexamer, involved in development andstress response, and regulated by pH and binding of Ca2+/calmodulin(CaM) to the C-terminal domain. We determined the crystal structure ofArabidopsis thaliana Gad1 in its CaM-free state, obtained a low-resolutionstructure of the calmodulin-activated Gad complex by small-angle X-rayscattering and identified the crucial residues, in the C-terminal domain, forregulation by pH and CaM binding
A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase
DOMINICI, Paola;PILATI, Stefania;ASTEGNO, Alessandra;
2009-01-01
Abstract
Glutamate decarboxylase (Gad) catalyzes glutamate to γ-aminobutyrateconversion. Plant Gad is a ∼340 kDa hexamer, involved in development andstress response, and regulated by pH and binding of Ca2+/calmodulin(CaM) to the C-terminal domain. We determined the crystal structure ofArabidopsis thaliana Gad1 in its CaM-free state, obtained a low-resolutionstructure of the calmodulin-activated Gad complex by small-angle X-rayscattering and identified the crucial residues, in the C-terminal domain, forregulation by pH and CaM binding
File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
