7YOB
Crystal structure of Aldehyde dehydrogenase 1A1 from mouse
Summary for 7YOB
Entry DOI | 10.2210/pdb7yob/pdb |
Descriptor | Aldehyde dehydrogenase 1A1 (1 entity in total) |
Functional Keywords | oxidoreductase |
Biological source | Mus musculus (house mouse) |
Total number of polymer chains | 8 |
Total formula weight | 442907.82 |
Authors | Zhang, X.Y.,Ouyang, Z.Q. (deposition date: 2022-08-01, release date: 2022-08-17, Last modification date: 2023-11-29) |
Primary citation | Zhang, X.,Ouyang, Z. Crystal structure of aldehyde dehydrogenase 1A1 from mouse. Biochem.Biophys.Res.Commun., 628:141-146, 2022 Cited by PubMed Abstract: Aldehyde dehydrogenase 1A1 (ALDH1A1) is an enzyme that catalyzes the NAD-dependent oxidation of aldehydes to carboxylic acids, participating in various metabolic processes. Currently, only structures from human and Ovis aries have been reported. Here we show a 2.89 Å resolution structure of ALDH1A1 from mice using X-ray crystallography. We performed a detailed analysis of the structure and compared it with ALDH1A1 structures from two other species, highlighting the significance of the differences. Structural superimposition reveals that the tetrameric molecule is asymmetrical, and the NAD-binding domain exhibits a certain rotation. In addition, the noticeable structural differences were detected, including the unique contact between Ser461 and Asp148, as well as the side chain orientations of three amino acids residues, Asn474, Met471 and Phe466. This study helps to expand the structural diversity of the ALDH family. PubMed: 36084552DOI: 10.1016/j.bbrc.2022.08.054 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.89 Å) |
Structure validation
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