Structural highlights
Function
J3QW32_GALSU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Bitto E, Kim do J, Bingman CA, Kim HJ, Han BW, Phillips GN Jr. Crystal structure of tandem ACT domain-containing protein ACTP from Galdieria sulphuraria. Proteins. 2012 Aug;80(8):2105-9. doi: 10.1002/prot.24101. Epub 2012 Jun 7. PMID:22528523 doi:10.1002/prot.24101
