Premium
Crystal structure of tandem ACT domain‐containing protein ACTP from Galdieria sulphuraria
Author(s) -
Bitto Eduard,
Kim Do Jin,
Bingman Craig A.,
Kim HyunJung,
Han Byung Woo,
Phillips George N.
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24101
Subject(s) - dimer , protein domain , biology , domain (mathematical analysis) , protein structure , amino acid , crystal structure , structural genomics , crystallography , genetics , biochemistry , gene , chemistry , mathematical analysis , mathematics , organic chemistry
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; © 2012 Wiley Periodicals, Inc.