Dreyer M K, Schulz G E
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.
J Mol Biol. 1993 Jun 5;231(3):549-53. doi: 10.1006/jmbi.1993.1307.
The three-dimensional structure of L-fuculose-1-phosphate aldolase (FucA) from Escherichia coli was determined by X-ray crystallography at a resolution of 2.13 A. The enzyme is a homotetramer with an M(r) of 23,775 per subunit. Since its activity depends on the presence of metal ions (Zn2+) the enzyme belongs to the class II aldolases. As expected from amino acid sequence comparisons, this first structure of a class II aldolase shows no similarity to the known structures of class I aldolases. It has some unusual features concerning the overall chain fold, the quaternary structure, and the co-ordination of the catalytically active zinc ion. A sequence comparison with the data bank indicated that the middle domain of the enzyme L-ribulose-5-phosphate-4-epimerase is homologous to FucA and may contain an active-center metal ion.
通过X射线晶体学以2.13埃的分辨率测定了来自大肠杆菌的L-岩藻糖-1-磷酸醛缩酶（FucA）的三维结构。该酶是一种同四聚体，每个亚基的分子量为23,775。由于其活性依赖于金属离子（Zn2+）的存在，该酶属于II类醛缩酶。正如氨基酸序列比较所预期的那样，这种II类醛缩酶的首个结构与已知的I类醛缩酶结构没有相似性。它在整体链折叠、四级结构以及催化活性锌离子的配位方面具有一些不寻常的特征。与数据库的序列比较表明，L-核糖ulose-5-磷酸-4-表异构酶的中间结构域与FucA同源，并且可能含有一个活性中心金属离子。
