Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase
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DOI：
10.1038/sj.emboj.7601410
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发表时间：
2006-11-15
期刊：
影响因子：
11.4
通讯作者：
Mueller, David M.
中科院分区：
文献类型：
--
作者：
Kabaleeswaran, Venkataraman;Puri, Neeti;Mueller, David M.
酵母线粒体F-1 ATP酶的晶体结构包含该复合物的三个独立拷贝，其中两个具有相似的构象，而第三个在相对于α（3）β（3）亚组装体的中心柄的位置上不同。所有三个副本显示非常相似的不对称特征观察到的牛酶，但酵母F-1 ATP酶结构提供了新的信息。特别是，牛F-1 ATP酶中结合ADP的活性位点结合有ATP类似物，因此该结构不代表ADP抑制形式。此外，其中一种复合物在无核苷酸的催化位点结合磷酸盐，与其他结构的比较提供了磷酸盐基团在初始结合和随后的催化过程中的运动的图片。在位置的中心柄之间的两个酵母F-1 ATP酶的三个副本，当这些结构相比，牛的酶的位置的变化提供了新的见解旋转催化过程中发生的构象变化。
The crystal structure of yeast mitochondrial F-1 ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the alpha(3)beta(3) sub-assembly. All three copies display very similar asymmetric features to those observed for the bovine enzyme, but the yeast F-1 ATPase structures provide novel information. In particular, the active site that binds ADP in bovine F-1 ATPase has an ATP analog bound and therefore this structure does not represent the ADP-inhibited form. In addition, one of the complexes binds phosphate in the nucleotide-free catalytic site, and comparison with other structures provides a picture of the movement of the phosphate group during initial binding and subsequent catalysis. The shifts in position of the central stalk between two of the three copies of yeast F-1 ATPase and when these structures are compared to those of the bovine enzyme give new insight into the conformational changes that take place during rotational catalysis.