6h1p

Publication Abstract from PubMed

Crystal structures of cold-adapted beta-D-galactosidase (EC 3.2.1.23) from the Antarctic bacterium Arthrobacter sp. 32cB (ArthbetaDG) have been determined in an unliganded form resulting from diffraction experiments conducted at 100K (at resolution 1.8A) and at room temperature (at resolution 3.0A). 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 ArthbetaDG 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.

Structural features of cold-adapted dimeric GH2 beta-D-galactosidase from Arthrobacter sp. 32cB.,Rutkiewicz M, Bujacz A, Bujacz G Biochim Biophys Acta Proteins Proteom. 2019 Jun 10. pii: S1570-9639(19)30103-7., doi: 10.1016/j.bbapap.2019.06.001. PMID:31195142^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.