Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F_1-ATPase

John V. Bason; Martin G. Montgomery; Andrew G. W. LeslieJohn E. Walker

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Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F_1-ATPase

机译：Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F_1-ATPase

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The hydrolysis of ATP by the ATP synthase in mitochondria is inhibited by a protein called IF_1. Bovine IF_1 has 84 amino acids, and its N-terminal inhibitory region is intrinsically disordered. In a known structure of bovine F_1-ATPase inhibited with residues 1-60 of IF_1, the inhibitory region from residues 1-50 is mainly α-helical and buried deeply at the α_(DP)β_(DP)-catalytic interface, where it forms extensive interactions with five of the nine subunits of F_1-ATPase but mainly with the β_(DP)-subunit. As described here, on the basis of two structures of inhibited complexes formed in the presence of large molar excesses of residues 1-60 of IF_1 and of a version of IF_1 with the mutation K39A, it appears that the intrinsically disordered inhibitory region interacts first with the αEβE-catalytic interface, the most open of the three catalytic interfaces, where the available interactions with the enzyme allow it to form an α-helix from residues 31-49. Then, in response to the hydrolysis of an ATP molecule and the associated partial closure of the interface to the α_(TP)β_(TP) state, the extent of the folded α-helical region of IF_1 increases to residues 23-50 as more interactions with the enzyme become possible. Finally, in response to the hydrolysis of a second ATP molecule and a concomitant 120° rotation of the γ-subunit, the interface closes further to the α_(DP)β_(DP)-state, allowing more interactions to form between the enzyme and IF_1. The structure of IF_1 now extends to its maximally folded state found in the previously observed inhibited complex.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2014年第31期|11305-11310|共6页
作者
John V. Bason; Martin G. Montgomery; Andrew G. W. LeslieJohn E. Walker;
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作者单位

The Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom;

The Medical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
rotary catalysis; inhibitory path; folding; binding site;

Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F_1-ATPase

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