1A4S

BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER

1A4S の概要

• エントリーDOI: 10.2210/pdb1a4s/pdb
• 分子名称: BETAINE ALDEHYDE DEHYDROGENASE (2 entities in total)
• 機能のキーワード: oxidoreductase, aldehyde oxidation
• 由来する生物種: Gadus callarias (Baltic cod)
• 細胞内の位置: Cytoplasm : P56533
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 217689.59

構造登録者

Johansson, K.,El Ahmad, M.,Hjelmqvist, L.,Ramaswamy, S.,Jornvall, H.,Eklund, H. (登録日: 1998-02-03, 公開日: 1998-04-08, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)