Dataset Information


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

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.


PROVIDER: S-EPMC4226431 | BioStudies | 2012-01-01

REPOSITORIES: biostudies

Similar Datasets

2009-01-01 | S-EPMC2742680 | BioStudies
2011-01-01 | S-EPMC3010194 | BioStudies
2007-01-01 | S-EPMC3871842 | BioStudies
2015-01-01 | S-EPMC4316638 | BioStudies
2018-01-01 | S-EPMC5880011 | BioStudies
| PRJNA315467 | ENA
| PRJDB11851 | ENA
2017-01-01 | S-EPMC5591647 | BioStudies
| PRJNA330791 | ENA
| PRJNA350520 | ENA