Work

Crystal structure of γ-carbonic anhydrase from the polyextremophilic bacterium Aeribacillus pallidus

Year: 2024

Type: article

Abstract: hydration activity in γ-apCA. Additionally, the structure reveals noncatalytic zinc and sulfate ions trapped at the trimer core and trimer-trimer noncrystallographic interfaces. These may contribute to stabilizing enzyme assembly and promoting crystal packing.

Source: Molecules and Cells

DOI: 10.1016/j.mocell.2024.100165

Authors: Seung Hun Choi, Mi Sun Jin

Institution: Gwangju Institute of Science and Technology

Language: English

Topic: Enzyme function and inhibition

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $2,500

Funder: National Research Foundation of Korea