6H1P

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

Summary for 6H1P

• Entry DOI: 10.2210/pdb6h1p/pdb
• Related: 6etz
• Descriptor: Beta-galactosidase, SODIUM ION (3 entities in total)
• Functional Keywords: beta-galactosidase, cold-adapted, psychrophilic, dimer, hydrolase, gh 2 family
• Biological source: Arthrobacter sp. 32cB
• Total number of polymer chains: 1
• Total formula weight: 107791.28

Authors

Rutkiewicz, M.,Bujacz, A.,Bujacz, G. (deposition date: 2018-07-12, release date: 2019-06-26, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.009 Å)