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EnglishGlutamate 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
| Titolo: | A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase |
| Autori: | |
| Data di pubblicazione: | 2009 |
| Rivista: | |
| 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 |
| Handle: | http://hdl.handle.net/11562/332997 |
| Appare nelle tipologie: | 01.01 Articolo in Rivista |
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