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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The structure of bovine F_1-ATPase complexed with the peptide antibiotic efrapeptin
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The structure of bovine F_1-ATPase complexed with the peptide antibiotic efrapeptin

机译:牛F_1-ATPase与肽抗菌素efrapeptin复合的结构

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摘要

In the previously determined structure of mitochondrial F_1-ATPase determined with crystals grown in the presence of adenylyl-imidodiphosphate (AMP-PNP) and ADP, the three catalytic β-subunits have different conforma- tions and nucleotide occupancies. AMP-PNP and ADP are bound to subunits β_TP and β_DP, respectively, and the third β-subunit (β_E) has no bound nucleotide. The efrapeptins are a closely related family of modified linear peptides containing 15 amino acids that inhibit both ATP synthesis and hydrolysis by binding to the F_1 catalytic domain of F_1F_o-ATP synthase.
机译:在先前确定的线粒体F_1-ATPase结构中,该结构是通过在腺苷酸-亚氨基二磷酸(AMP-PNP)和ADP存在下生长的晶体确定的,三个催化性β-亚基具有不同的构型和核苷酸占有率。 AMP-PNP和ADP分别与亚基β_TP和β_DP结合,并且第三个β亚基(β_E)没有结合核苷酸。 rapepteptins是一个密切相关的修饰线性肽家族,包含15个氨基酸,这些氨基酸通过与F_1F_o-ATP合酶的F_1催化域结合而抑制ATP合成和水解。

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