Publication Abstract from PubMed
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. Proteins 2012; (c) 2012 Wiley Periodicals, Inc.
Crystal structure of tandem ACT domain-containing protein ACTP from Galdieria sulphuraria.,Bitto E, Kim do J, Bingman CA, Kim HJ, Han BW, Phillips GN Jr Proteins. 2012 Aug;80(8):2105-9. doi: 10.1002/prot.24101. Epub 2012 Jun 7. PMID:22528523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
