6ENZ

Crystal structure of mouse GADL1

6ENZ の概要

• エントリーDOI: 10.2210/pdb6enz/pdb
• 分子名称: Acidic amino acid decarboxylase GADL1, PYRIDOXAL-5'-PHOSPHATE (2 entities in total)
• 機能のキーワード: decarboxylase, homodimer, pyridoxal phosphate, lyase
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121401.58

構造登録者

Raasakka, A.,Mahootchi, E.,Winge, I.,Luan, W.,Kursula, P.,Haavik, J. (登録日: 2017-10-07, 公開日: 2018-01-03, 最終更新日: 2024-01-31)

主引用文献

Raasakka, A.,Mahootchi, E.,Winge, I.,Luan, W.,Kursula, P.,Haavik, J.
Structure of the mouse acidic amino acid decarboxylase GADL1.
Acta Crystallogr F Struct Biol Commun, 74:65-73, 2018

PubMed Abstract: Pyridoxal 5'-phosphate (PLP) is a ubiquitous cofactor in various enzyme classes, including PLP-dependent decarboxylases. A recently discovered member of this class is glutamic acid decarboxylase-like protein 1 (GADL1), which lacks the activity to decarboxylate glutamate to γ-aminobutyrate, despite its homology to glutamic acid decarboxylase. Among the acidic amino acid decarboxylases, GADL1 is most similar to cysteine sulfinic acid decarboxylase (CSAD), but the physiological function of GADL1 is unclear, although its expression pattern and activity suggest a role in neurotransmitter and neuroprotectant metabolism. The crystal structure of mouse GADL1 is described, together with a solution model based on small-angle X-ray scattering data. While the overall fold and the conformation of the bound PLP are similar to those in other PLP-dependent decarboxylases, GADL1 adopts a more loose conformation in solution, which might have functional relevance in ligand binding and catalysis. The structural data raise new questions about the compactness, flexibility and conformational dynamics of PLP-dependent decarboxylases, including GADL1.

PubMed: 29372909
DOI: 10.1107/S2053230X17017848

実験手法

X-RAY DIFFRACTION (3 Å)