6H1P

Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB - data collected at room temperature

6H1P の概要

• エントリーDOI: 10.2210/pdb6h1p/pdb
• 関連するPDBエントリー: 6etz
• 分子名称: Beta-galactosidase, SODIUM ION (3 entities in total)
• 機能のキーワード: beta-galactosidase, cold-adapted, psychrophilic, dimer, hydrolase, gh 2 family
• 由来する生物種: Arthrobacter sp. 32cB
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 107791.28

構造登録者

Rutkiewicz, M.,Bujacz, A.,Bujacz, G. (登録日: 2018-07-12, 公開日: 2019-06-26, 最終更新日: 2024-01-17)

主引用文献

Rutkiewicz, M.,Bujacz, A.,Bujacz, G.
Structural features of cold-adapted dimeric GH2 beta-D-galactosidase from Arthrobacter sp. 32cB.
Biochim Biophys Acta Proteins Proteom, 1867:776-786, 2019

PubMed Abstract: Crystal structures of cold-adapted β-d-galactosidase (EC 3.2.1.23) from the Antarctic bacterium Arthrobacter sp. 32cB (ArthβDG) have been determined in an unliganded form resulting from diffraction experiments conducted at 100 K (at resolution 1.8 Å) and at room temperature (at resolution 3.0 Å). A detailed comparison of those two structures of the same enzyme was performed in order to estimate differences in their molecular flexibility and rigidity and to study structural rationalization for the cold-adaptation of the investigated enzyme. Furthermore, a comparative analysis with structures of homologous enzymes from psychrophilic, mesophilic, and thermophilic sources has been discussed to elucidate the relationship between structure and cold-adaptation in a wider context. The performed studies confirm that the structure of cold-adapted ArthβDG maintains balance between molecular stability and structural flexibility, which can be observed independently on the temperature of conducted X-ray diffraction experiments. Obtained information about proper protein function under given conditions provide a guideline for rational engineering of proteins in terms of their temperature optimum and thermal stability.

PubMed: 31195142
DOI: 10.1016/j.bbapap.2019.06.001

実験手法

X-RAY DIFFRACTION (3.009 Å)