Structure of the mouse acidic amino acid decarboxylase GADL1
|Author:||Raasakka, Arne1; Mahootchi, Elaheh1,2; Winge, Ingeborg1,2;|
1Department of Biomedicine, University of Bergen, Jonas Lies Vei 91, 5009 Bergen, Norway
2K. G. Jebsen Centre for Research on Neuropsychiatric Disorders, University of Bergen, Jonas Lies Vei 91, 5009 Bergen, Norway
3Faculty of Biochemistry and Molecular Medicine, University of Oulu, PO Box 5400, 90014 Oulu, Finland
4Division of Psychiatry, Haukeland University Hospital, Bergen, Norway
|Online Access:||PDF Full Text (PDF, 2.7 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe201803125851
John Wiley & Sons,
|Publish Date:|| 2018-03-12
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.
Acta crystallographica. Section F, Structural biology communications
|Pages:||65 - 73|
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
Funding for this research was provided by: Helse Vest (grant to Jan Haavik); Norges Forskningsråd (grant to Petri Kursula); Sigrid Juséliuksen Säätiö (grant to Petri Kursula); Stiftelsen Kristian Gerhard Jebsen (grant to Jan Haavik); Seventh Framework Programme (grant No. 602805 to Jan Haavik).
© 2018 The Authors. Creative Commons Attribution (CC-BY) Licence.