Park Ae Kyung, Lee Jeong Hye, Chi Young Min, Moon Jin Ho
Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):78-80. doi: 10.1107/S1744309111049426. Epub 2011 Dec 24.
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%.
烯酰-（酰基载体蛋白）还原酶（ENR）催化细菌脂肪酸生物合成（FAS II）途径中脂肪酸延伸循环的最后一步。最近，已从霍乱弧菌中鉴定出一类新的ENR，并将其命名为FabV。为了在结构水平上了解这类新型ENR的分子机制，费氏弧菌的FabV被过量表达、纯化并结晶。从天然晶体收集了分辨率为2.7 Å的衍射数据。该晶体属于正交晶系空间群P2(1)2(1)2，晶胞参数a = 123.53，b = 164.14，c = 97.07 Å。不对称单元中存在四个FabV分子，V(M)值为2.81 Å(3) Da(-1)，相应的溶剂含量为54.5%。
