ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.
(2010) In Structure 18(3). p.354-365- Abstract
- Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) 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 A, 14 A, and 13 A 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... (More)
- Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) 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 A, 14 A, and 13 A 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. (Less)
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https://lup.lub.lu.se/record/1582248
- author
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Structure
- volume
- 18
- issue
- 3
- pages
- 354 - 365
- publisher
- Cell Press
- external identifiers
-
- wos:000275492000012
- pmid:20223218
- scopus:77649111713
- pmid:20223218
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2010.01.001
- language
- English
- LU publication?
- yes
- id
- 6333b7f9-901e-42cb-bf22-c759f7b5e2e2 (old id 1582248)
- date added to LUP
- 2016-04-01 10:26:49
- date last changed
- 2022-04-27 22:08:36
@article{6333b7f9-901e-42cb-bf22-c759f7b5e2e2, abstract = {{Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) 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 A, 14 A, and 13 A 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.}}, author = {{Lundqvist, Joakim and Elmlund, Hans and Peterson Wulff, Ragna and Berglund, Lisa and Elmlund, Dominika and Emanuelsson, Cecilia and Hebert, Hans and Willows, Robert D and Hansson, Mats and Lindahl, Martin and Al-Karadaghi, Salam}}, issn = {{0969-2126}}, language = {{eng}}, number = {{3}}, pages = {{354--365}}, publisher = {{Cell Press}}, series = {{Structure}}, title = {{ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.}}, url = {{http://dx.doi.org/10.1016/j.str.2010.01.001}}, doi = {{10.1016/j.str.2010.01.001}}, volume = {{18}}, year = {{2010}}, }