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Proteins. 2012 Aug;80(8):2105-2109. doi: 10.1002/prot.24101. Epub 2012 Jun 7.

Crystal structure of tandem ACT domain-containing protein ACTP from Galdieria sulphuraria.

Author information

1
Department of Chemistry and Biochemistry, Georgian Court University, Lakewood, New Jersey 08701, USA.
2
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea.
3
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
4
College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea.
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Contributed equally

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.

PMID:
22528523
PMCID:
PMC4226431
DOI:
10.1002/prot.24101
[Indexed for MEDLINE]
Free PMC Article

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