The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF₁.

The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF₁.
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DOI:
10.1098/rsob.120164
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发表时间:
2013-02-13
期刊:
影响因子:
5.8
通讯作者:
Walker JE
Walker JE
中科院分区:
生物学2区
文献类型:
--
作者:
Robinson GC;Bason JV;Montgomery MG;Fearnley IM;Mueller DM;Leslie AG;Walker JE

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在2.5 μ m分辨率下测定了被IF_1抑制的酿酒酵母F_1-ATP酶的结构。IF 1的抑制区从残基1到36被截留在酶的三个催化界面之一的αDP-和β DP-亚基的C-末端结构域之间。虽然抑制复合物的结构与牛抑制复合物的结构相似,但抑制剂的结构及其与F1-ATP酶的详细相互作用之间存在显着差异。然而,最显著的差异是催化β E亚基的核苷酸占有率。酵母复合物中β E亚基上的核苷酸结合位点含有ADP分子,但没有伴随的镁离子,而牛复合物中该位点未被占据。因此,该结构提供了产物顺序释放的进一步证据,其中磷酸根和镁离子在ADP分子之前释放。
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined at 2.5 Å resolution. The inhibitory region of IF1 from residues 1 to 36 is entrapped between the C-terminal domains of the αDP- and βDP-subunits in one of the three catalytic interfaces of the enzyme. Although the structure of the inhibited complex is similar to that of the bovine-inhibited complex, there are significant differences between the structures of the inhibitors and their detailed interactions with F1-ATPase. However, the most significant difference is in the nucleotide occupancy of the catalytic βE-subunits. The nucleotide binding site in βE-subunit in the yeast complex contains an ADP molecule without an accompanying magnesium ion, whereas it is unoccupied in the bovine complex. Thus, the structure provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.
DOI: 10.1107/s090744491003982x
发表时间: 2011-04
期刊: Acta crystallographica. Section D, Biological crystallography
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