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Crystal structure of tandem ACT domain-containing protein ACTP from Galdieria sulphuraria
- Authors
- Bitto, Eduard; Kim, Do Jin; Bingman, Craig A.; Kim, Hyun-Jung; Han, Byung Woo; Phillips, George N., Jr.
- Issue Date
- Aug-2012
- Publisher
- WILEY-BLACKWELL
- Keywords
- ACT domain; ACT domain-containing protein; Galdieria sulphuraria
- Citation
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.80, no.8, pp 2105 - 2109
- Pages
- 5
- Journal Title
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Volume
- 80
- Number
- 8
- Start Page
- 2105
- End Page
- 2109
- ISSN
- 0887-3585
1097-0134
- 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. Proteins 2012; (c) 2012 Wiley Periodicals, Inc.
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