Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/120261
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- Title
- ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase
- Related
- Structure, Vol. 18, Issue 3 (2010), p.354-365
- DOI
- 10.1016/j.str.2010.01.001
- Publisher
- Cell Press
- Date
- 2010
- FoR/RFCD Code(s)
-
060100 Biochemistry and Cell Biology
- Author/Creator
- Lundqvist, Joakim
- Author/Creator
- Elmlund, Hans
- Author/Creator
- Al-Karadaghi, Salam
- Author/Creator
- Peterson Wulff, Ragna
- Author/Creator
- Berglund, Lisa
- Author/Creator
- Elmlund, Dominika
- Author/Creator
- Emanuelsson, Cecilia
- Author/Creator
- Herbert, Hans
- Author/Creator
- Willows, Robert D
- Author/Creator
- Hansson, Mats
- Author/Creator
- Lindahl, Martin
- Description
- 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.
- Description
- 12 page(s)
- Subject Keyword
- 060100 Biochemistry and Cell Biology
- Subject Keyword
- magnesium chelatase
- Subject Keyword
- chlorophyll synthesis
- Subject Keyword
- bacteriochlorophyll
- Resource Type
- journal article
- Organisation
- Macquarie University. Dept. of Chemistry and Biomolecular Sciences
- Identifier
- http://hdl.handle.net/1959.14/120261
- Identifier
- ISSN:0969-2126
- Identifier
- mq-rm-2009011261
- Language
- eng
- Reviewed
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