Crystal structure of SCO6571 from Streptomyces coelicolor A3(2).
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.
Begum
Parvin
P
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.
Sakai
Naoki
N
Hayashi
Takeshi
T
Gao
Yong-Gui
YG
Tamura
Tomohiro
T
Watanabe
Nobuhisa
N
Yao
Min
M
Tanaka
Isao
I
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D048372:Streptomyces coelicolor / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins