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Crystal structure of tandem ACT domain-containing protein ACTP from Galdieria sulphuraria
Eduard Bitto1, Do Jin Kim2, Craig A Bingman3
1Department of Chemistry and Biochemistry, Georgian Court University, Lakewood, New Jersey 08701, USA.
Abstract:
The ACT domain is a structurally conserved small molecule binding domain which is mostly involved in amino acid and purine metabolism. Here, we report the crystal structure of a tandem ACT domain-containing protein (ACTP) from Galdieria sulphuraria. The two ACTP monomers in the asymmetric unit form a dimer with a non-crystallographic twofold axis in a domain-swapped manner, showing a horseshoe-like structure with a central crevice. This structure contributes to expand our knowledge on the structural diversity of ACT domain-containing proteins.
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