1A4S

BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER

Summary for 1A4S

• Entry DOI: 10.2210/pdb1a4s/pdb
• Descriptor: BETAINE ALDEHYDE DEHYDROGENASE (2 entities in total)
• Functional Keywords: oxidoreductase, aldehyde oxidation
• Biological source: Gadus callarias (Baltic cod)
• Cellular location: Cytoplasm : P56533
• Total number of polymer chains: 4
• Total formula weight: 217689.59

Authors

Johansson, K.,El Ahmad, M.,Hjelmqvist, L.,Ramaswamy, S.,Jornvall, H.,Eklund, H. (deposition date: 1998-02-03, release date: 1998-04-08, Last modification date: 2024-05-22)

Primary citation

Johansson, K.,El-Ahmad, M.,Ramaswamy, S.,Hjelmqvist, L.,Jornvall, H.,Eklund, H.
Structure of betaine aldehyde dehydrogenase at 2.1 A resolution.
Protein Sci., 7:2106-2117, 1998

PubMed Abstract: The three-dimensional structure of betaine aldehyde dehydrogenase, the most abundant aldehyde dehydrogenase (ALDH) of cod liver, has been determined at 2.1 A resolution by the X-ray crystallographic method of molecular replacement. This enzyme represents a novel structure of the highly multiple ALDH, with at least 12 distinct classes in humans. This betaine ALDH of class 9 is different from the two recently determined ALDH structures (classes 2 and 3). Like these, the betaine ALDH structure has three domains, one coenzyme binding domain, one catalytic domain, and one oligomerization domain. Crystals grown in the presence or absence of NAD+ have very similar structures and no significant conformational change occurs upon coenzyme binding. This is probably due to the tight interactions between domains within the subunit and between subunits in the tetramer. The oligomerization domains link the catalytic domains together into two 20-stranded pleated sheet structures. The overall structure is similar to that of the tetrameric bovine class 2 and dimeric rat class 3 ALDH, but the coenzyme binding with the nicotinamide in anti conformation, resembles that of class 2 rather than of class 3.

PubMed: 9792097

Experimental method

X-RAY DIFFRACTION (2.1 Å)