4GAC

High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form

Summary for 4GAC

• Entry DOI: 10.2210/pdb4gac/pdb
• Descriptor: Alcohol dehydrogenase [NADP(+)], 1,2-ETHANEDIOL, CITRATE ANION, ... (4 entities in total)
• Functional Keywords: tim barrel, aldheyde reductase akr1a4, smar1, oxidoreductase
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 2
• Total formula weight: 73513.69

Authors

Faucher, F.,Jia, Z. (deposition date: 2012-07-25, release date: 2012-11-07, Last modification date: 2023-09-13)

Primary citation

Faucher, F.,Jia, Z.
High-resolution structure of AKR1a4 in the apo form and its interaction with ligands.
Acta Crystallogr.,Sect.F, 68:1271-1274, 2012

PubMed Abstract: Aldo-keto reductase 1a4 (AKR1a4; EC 1.1.1.2) is the mouse orthologue of human aldehyde reductase (AKR1a1), the founding member of the AKR family. As an NADPH-dependent enzyme, AKR1a4 catalyses the conversion of D-glucuronate to L-gulonate. AKR1a4 is involved in ascorbate biosynthesis in mice, but has also recently been found to interact with SMAR1, providing a novel mechanism of ROS regulation by ATM. Here, the crystal structure of AKR1a4 in its apo form at 1.64 Å resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented.

PubMed: 23143230
DOI: 10.1107/S1744309112037128

Experimental method

X-RAY DIFFRACTION (1.64 Å)