Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2)

Title: Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2)

Volume: 15 Issue: 7

Author(s): Parvin Begum, Naoki Sakai, Takeshi Hayashi, Yong-Gui Gao, Tomohiro Tamura, Nobuhisa Watanabe, Min Yao and Isao Tanaka

Affiliation:

Keywords: Crystal structure analysis, Streptomyces coelicolor A3(2), xylose isomerase-like superfamily, D3 symmetry

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 Å and were found to belong to the orthorhombic space group P212121 with unit cell parameters a = 84.5, b = 171.6, c = 184.8 Å. Six molecules in the asymmetric unit give a crystal volume per protein mass (VM) of 2.97 Å3 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 D3 symmetry.

Cite this article as:

Begum Parvin, Sakai Naoki, Hayashi Takeshi, Gao Yong-Gui, Tamura Tomohiro, Watanabe Nobuhisa, Yao Min and Tanaka Isao, Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2), Protein & Peptide Letters 2008; 15 (7) . https://dx.doi.org/10.2174/092986608785133636