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- W1982024223 abstract "Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg2+ into protoporphyrin IX (PPIX). Here we report the reconstruction using single-particle cryo-electron microscopy of the complex between subunits BchD and BchI of Rhodobacter capsulatus Mg-chelatase in the presence of ADP, the nonhydrolyzable ATP analog AMPPNP, and ATP at 7.5 Å, 14 Å, and 13 Å resolution, respectively. We show that the two AAA+ modules of the subunits form a unique complex of 3 dimers related by a three-fold axis. The reconstructions demonstrate substantial differences between the conformations of the complex in the presence of ATP and ADP, and suggest that the C-terminal integrin-I domains of the BchD subunits play a central role in transmitting conformational changes of BchI to BchD. Based on these data a model for the function of magnesium chelatase is proposed." @default.
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- W1982024223 date "2010-03-01" @default.
- W1982024223 modified "2023-10-17" @default.
- W1982024223 title "ATP-Induced Conformational Dynamics in the AAA+ Motor Unit of Magnesium Chelatase" @default.
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- W1982024223 doi "https://doi.org/10.1016/j.str.2010.01.001" @default.
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