Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of SCO6571 from Streptomyces coelicolor A3(2).,Begum P, Sakai N, Hayashi T, Gao YG, Tamura T, Watanabe N, Yao M, Tanaka I Protein Pept Lett. 2008;15(7):709-12. PMID:18782066[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Begum P, Sakai N, Hayashi T, Gao YG, Tamura T, Watanabe N, Yao M, Tanaka I. Crystal structure of SCO6571 from Streptomyces coelicolor A3(2). Protein Pept Lett. 2008;15(7):709-12. PMID:18782066
