Amano T, Yoshida M, Matsuo Y, Nishikawa K
Research Laboratory of Resources Utilization, R-1, Tokyo Institute of Technology, Yokohama, Japan.
FEBS Lett. 1994 Aug 29;351(1):1-5. doi: 10.1016/0014-5793(94)00796-9.
In contrast to the previous topological model of the ATP binding domain of the F1-ATPase beta subunit based on analogies to those of ras p21 and adenylate kinase, a more consistent model can be constructed with the known structure of the recA protein as a reference. The secondary structure of the F1-ATPase beta subunit predicted from the primary structure agrees well with that of the recA protein. The topology includes a repetitive beta alpha c beta alpha beta alpha beta alpha beta structure where all beta strands are parallel and surround the central alpha c helix above which bound ATP is located. Several residues thought to be located at catalytic site as reported in genetic and chemical labeling work can be consistently positioned in this model.
与之前基于与ras p21和腺苷酸激酶类似性构建的F1 - ATP合酶β亚基ATP结合结构域的拓扑模型不同，可以以recA蛋白的已知结构为参考构建一个更连贯的模型。从一级结构预测的F1 - ATP合酶β亚基的二级结构与recA蛋白的二级结构非常吻合。其拓扑结构包括一个重复的β-α-c-β-α-β-α-β-α-β结构，其中所有β链都是平行的，并围绕着中央α-c螺旋，结合的ATP位于该螺旋上方。在该模型中，可以将遗传和化学标记研究中报道的几个被认为位于催化位点的残基进行连贯定位。
