4RQT

Alcohol Dehydrogenase Crystal Structure

Summary for 4RQT

• Entry DOI: 10.2210/pdb4rqt/pdb
• Related: 4RQU
• Descriptor: Alcohol dehydrogenase class-P, ZINC ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: rossmann fold, alcohol dehydrogenase, oxidoreductase
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cytoplasm: P06525
• Total number of polymer chains: 1
• Total formula weight: 41317.66

Authors

Xu, Y.W. (deposition date: 2014-11-05, release date: 2014-12-17, Last modification date: 2023-09-20)

Primary citation

Chen, F.,Wang, P.,An, Y.,Huang, J.,Xu, Y.
Structural insight into the conformational change of alcohol dehydrogenase from arabidopsis Thalianal during coenzyme binding.
Biochimie, 108C:33-39, 2014

PubMed Abstract: Alcohol dehydrogenase (ADH, EC 1.1.1.1) plays important roles in the metabolism of alcohols and aldehydes. They are often subjected to conformational changes that are critical for the enzymatic activity and have received intensive investigation for horse liver ADH. However, for the large plant ADH members, little is known regarding both the conformational change and its relationship to catalytic activity as plant ADH structures were rarely available. Here we describe three Arabidopsis ADH conformations obtained from two crystals, the apo crystal that was free of ligand, and the complex crystal that was with NAD. The NAD-complexed crystal yielded two different structural forms for the two subunits, one was occupied by the coenzyme, and the other was free and open. Structural comparisons demonstrate that the occupied subunit is in a closed conformation while the free subunit is fully open, and the apo structure in intermediate. Though all the forms have an overall fold similar to that of horse and human ADHs, the catalytic domain has an over 10° rotation. Additionally, unlike horse liver ADH, the loop (295-302aa) adopts different conformation. It does not rearrange upon the binding of the coenzyme norVal297 side chain experiences a flipping. Instead it always remains in the active site. His48 plays a switching role in the structure. Its imidazole ring has to swim away from the binding site to permit NAD binding. These together with the large differences in the substrate binding pocket, as well as in the proton relay system demonstrate that AtADH adopts a different catalysis mechanism from horse liver ADH.

PubMed: 25447145
DOI: 10.1016/j.biochi.2014.10.023

Experimental method

X-RAY DIFFRACTION (2.3 Å)