2ZDS

Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2)

Summary for 2ZDS

• Entry DOI: 10.2210/pdb2zds/pdb
• Descriptor: Putative DNA-binding protein (2 entities in total)
• Functional Keywords: tim-barrel fold, dna-binding, dna binding protein, structural genomics, nppsfa, national project on protein structural and functional analyses
• Biological source: Streptomyces coelicolor
• Total number of polymer chains: 6
• Total formula weight: 233805.59

Authors

Begum, P.,Gao, Y.G.,Sakai, N.,Yao, M.,Watanabe, N.,Tanaka, I. (deposition date: 2007-11-27, release date: 2008-12-02, Last modification date: 2019-10-16)

Primary citation

Begum, P.,Sakai, N.,Hayashi, T.,Gao, Y.G.,Tamura, T.,Watanabe, N.,Yao, M.,Tanaka, I.
Crystal structure of SCO6571 from Streptomyces coelicolor A3(2).
Protein Pept.Lett., 15:709-712, 2008

PubMed Abstract: SCO6571 protein from Streptomyces coelicolor A3(2) was overexpressed and purified using Rhodococcus erythropolis as an expressing host. Crystals of selenomethionine-substituted SCO6571 have been obtained by vapor diffusion method. SCO6571 crystals diffract to 2.3 A and were found to belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell parameters a = 84.5, b = 171.6, c = 184.8 A. Six molecules in the asymmetric unit give a crystal volume per protein mass (V(M)) of 2.97 A (3) Da(-1) and solvent content of 58.6 %. The structure was solved by the single wavelength anomalous diffraction (SAD) method. SCO6571 is a TIM-barrel fold protein that assembles into a hexameric molecule with D(3) symmetry.

PubMed: 18782066
DOI: 10.2174/092986608785133636

Experimental method

X-RAY DIFFRACTION (2.3 Å)