Crystal structure of tandem ACT domain‐containing protein ACTP from  Galdieria sulphuraria | Zendy

Bitto Eduard | Zendy; Kim Do Jin | Zendy; Bingman Craig A. | Zendy; Kim HyunJung | Zendy; Han Byung Woo | Zendy; Phillips George N. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research