Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae.
The enoyl-acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty-acid biosynthesis. Selenomethionine-substituted FabK was purified and crystallized by the hanging-drop vapour-diffusion method at 277 K. The crystal belongs to space group P2(1), with unit-cell parameters a = 50.26, b = 126.70, c = 53.63 A, beta = 112.46 degrees . Diffraction data were collected to 2.00 A resolution using synchrotron beamline BL32B2 at SPring-8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.
Saito
Jun
J
Pharmaceutical Research Center, Meiji Seika Kaisha Ltd, 760 Morooka-cho, Kohoku-ku, Yokohama 222-8567, Japan. jun_saito@meiji.co.jp
Yamada
Mototsugu
M
Watanabe
Takashi
T
Kitagawa
Hideo
H
Takeuchi
Yasuo
Y
D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization / Q000379:methods; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) / Q000737:chemistry*; D012645:Selenomethionine; D012997:Solvents; D013296:Streptococcus pneumoniae / Q000201:enzymology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D012997:Solvents; D012645:Selenomethionine; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)