Crystallization and preliminary X-ray crystallographic studies of a new class of enoyl-(acyl-carrier protein) reductase, FabV, from Vibrio fischeri.
Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named FabV. In order to understand the molecular mechanism of the new class of ENR at the structural level, FabV from V. fischeri was overexpressed, purified and crystallized. Diffraction data were collected to 2.7 Å resolution from a native crystal. The crystal belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07 Å. The presence of four molecules of FabV in the asymmetric unit gave a V(M) value of 2.81 Å(3) Da(-1), with a corresponding solvent content of 54.5%.
Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
Ae Kyung
AK
Park
Jeong Hye
JH
Lee
Young Min
YM
Chi
Jin Ho
JH
Moon
D048908:Aliivibrio fischeri / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry*
D044925:Oxidoreductases Acting on CH-CH Group Donors