› 2okk

X-ray diffraction
2.3Å resolution

The X-ray crystal structure of the 65kDa isoform of Glutamic Acid Decarboxylase (GAD65)

Released:
DOI: 10.2210/pdb2okk/pdb
PDB 2okk coloured by chain and viewed from the front.
PDB 2okk coloured by chain and viewed from the side.
PDB 2okk coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop.
Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC
Nat. Struct. Mol. Biol. 14 280-6 (2007)
PMID: 17384644

Function and Biology Details

Reaction catalysed: 
L-glutamate = 4-aminobutanoate + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate decarboxylase 2 Chain: A
Molecule details ›
Chain: A
Length: 497 amino acids
Theoretical weight: 56.78 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q05329 (Residues: 88-584; Coverage: 85%)
Gene names: GAD2, GAD65
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ABU 2 x ABU
Ligand GOL 1 x GOL
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 78.251Å b: 99.057Å c: 120.009Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.196 0.256
Expression system: Saccharomyces cerevisiae

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Citations

27 review citations

Stiff-person Syndrome and GAD Antibody-spectrum Disorders: GABAergic Neuronal Excitability, Immunopathogenesis and Update on Antibody Therapies.
Dalakas MC. (2022)
26 more

12 mentions without citation

A conserved mechanism of GABA binding and antagonism is revealed by structure-function analysis of the periplasmic binding protein Atu2422 in Agrobacterium tumefaciens.
Planamente et al. (2010)
11 more