5F2C

Thermostable aldehyde dehydrogenase from Pyrobaculum sp. 1860 crystallized in microgravity (complex with NADP+)

5F2C の概要

• エントリーDOI: 10.2210/pdb5f2c/pdb
• 関連するPDBエントリー: 4NMK
• 分子名称: Aldehyde dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: thermostable aldehyde dehydrogenase, oxidoreductase
• 由来する生物種: Pyrobaculum ferrireducens
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 441712.99

構造登録者

Petrova, T.E.,Bezsudnova, E.Y.,Boyko, K.M.,Mardanov, A.V.,Gumerov, V.M.,Ravin, N.V.,Popov, V.O. (登録日: 2015-12-01, 公開日: 2016-12-14, 最終更新日: 2024-01-10)

主引用文献

Bezsudnova, E.Y.,Petrova, T.E.,Artemova, N.V.,Boyko, K.M.,Shabalin, I.G.,Rakitina, T.V.,Polyakov, K.M.,Popov, V.O.
NADP-Dependent Aldehyde Dehydrogenase from ArchaeonPyrobaculum sp.1860: Structural and Functional Features.
Archaea, 2016:9127857-9127857, 2016

PubMed Abstract: We present the functional and structural characterization of the first archaeal thermostable NADP-dependent aldehyde dehydrogenase AlDHPyr1147. , AlDHPyr1147 catalyzes the irreversible oxidation of short aliphatic aldehydes at 60-85°С, and the affinity of AlDHPyr1147 to the NADP+ at 60°С is comparable to that for mesophilic analogues at 25°С. We determined the structures of the apo form of AlDHPyr1147 (3.04 Å resolution), three binary complexes with the coenzyme (1.90, 2.06, and 2.19 Å), and the ternary complex with the coenzyme and isobutyraldehyde as a substrate (2.66 Å). The nicotinamide moiety of the coenzyme is disordered in two binary complexes, while it is ordered in the ternary complex, as well as in the binary complex obtained after additional soaking with the substrate. AlDHPyr1147 structures demonstrate the strengthening of the dimeric contact (as compared with the analogues) and the concerted conformational flexibility of catalytic Cys287 and Glu253, as well as Leu254 and the nicotinamide moiety of the coenzyme. A comparison of the active sites of AlDHPyr1147 and dehydrogenases characterized earlier suggests that proton relay systems, which were previously proposed for dehydrogenases of this family, are blocked in AlDHPyr1147, and the proton release in the latter can occur through the substrate channel.

PubMed: 27956891
DOI: 10.1155/2016/9127857

実験手法

X-RAY DIFFRACTION (1.898 Å)