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ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.

Lundqvist, Joakim LU ; Elmlund, Hans LU ; Peterson Wulff, Ragna LU ; Berglund, Lisa; Elmlund, Dominika; Emanuelsson, Cecilia LU ; Hebert, Hans; Willows, Robert D; Hansson, Mats LU and Lindahl, Martin LU , et al. (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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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
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
2010-04-12 15:42:52
date last changed
2018-06-03 03:13:19
@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},
  volume       = {18},
  year         = {2010},
}