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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.

SUBMITTER: Bitto E

PROVIDER: S-EPMC4226431 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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

Bitto Eduard E Kim Do Jin DJ Bingman Craig A CA Kim Hyun-Jung HJ Han Byung Woo BW Phillips George N GN

Proteins 20120607 8

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 struct ...[more]

PMID: 22528523

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