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Basic information
Entry | Database: PDB / ID: 3hbx | ||||||
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Title | Crystal structure of GAD1 from Arabidopsis thaliana | ||||||
![]() | Glutamate decarboxylase 1 | ||||||
![]() | LYASE / Calmodulin-binding / Decarboxylase / Pyridoxal phosphate | ||||||
Function / homology | ![]() glutamate decarboxylase / glutamate decarboxylase activity / glutamate catabolic process / response to cadmium ion / pyridoxal phosphate binding / calmodulin binding / cytosol Similarity search - Function | ||||||
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Method | ![]() ![]() ![]() | ||||||
![]() | Gut, H. / Dominici, P. / Pilati, S. / Gruetter, M.G. / Capitani, G. | ||||||
![]() | ![]() Title: A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. Authors: Heinz Gut / Paola Dominici / Stefania Pilati / Alessandra Astegno / Maxim V Petoukhov / Dmitri I Svergun / Markus G Grütter / Guido Capitani / ![]() Abstract: Glutamate decarboxylase (Gad) catalyzes glutamate to gamma-aminobutyrate conversion. Plant Gad is a approximately 340 kDa hexamer, involved in development and stress response, and regulated by pH and ...Glutamate decarboxylase (Gad) catalyzes glutamate to gamma-aminobutyrate conversion. Plant Gad is a approximately 340 kDa hexamer, involved in development and stress response, and regulated by pH and binding of Ca(2+)/calmodulin (CaM) to the C-terminal domain. We determined the crystal structure of Arabidopsis thaliana Gad1 in its CaM-free state, obtained a low-resolution structure of the calmodulin-activated Gad complex by small-angle X-ray scattering and identified the crucial residues, in the C-terminal domain, for regulation by pH and CaM binding. CaM activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad1-CaM complex with an unusual 1:3 stoichiometry. The complex is loosely packed: thanks to the flexible linkers connecting the enzyme core with the six C-terminal regulatory domains, the CaM molecules retain considerable positional and orientational freedom with respect to Gad1. The complex thus represents a prototype for a novel CaM-target interaction mode. Thanks to its two levels of regulation, both targeting the C-terminal domain, Gad can respond flexibly to different kinds of cellular stress occurring at different pH values. | ||||||
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-Related structure data
Related structure data | ![]() 1pmmS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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