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Structure paper

TitleA common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase.
Journal, issue, pagesJ Mol Biol, Vol. 392, Issue 2, Page 334-351, Year 2009
Publish dateSep 18, 2009
AuthorsHeinz Gut / Paola Dominici / Stefania Pilati / Alessandra Astegno / Maxim V Petoukhov / Dmitri I Svergun / Markus G Grütter / Guido Capitani /
PubMed AbstractGlutamate 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.
External linksJ Mol Biol / PubMed:19580813
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.672 Å
Structure data

SASDAQ4:
6:3 complex of GAD:CaM (Calmodulin + Glutamate decarboxylase, GAD)
Method: SAXS/SANS

PDB-3hbx:
Crystal structure of GAD1 from Arabidopsis thaliana
Method: X-RAY DIFFRACTION / Resolution: 2.672 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Homo sapiens (human)
  • Petunia x hybrida (garden petunia)
  • arabidopsis thaliana (thale cress)
KeywordsLYASE / Calmodulin-binding / Decarboxylase / Pyridoxal phosphate

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