Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.
Journal, issue, pages	Structure, Vol. 18, Issue 3, Page 354-365, Year 2010
Publish date	Mar 10, 2010
Authors	Joakim Lundqvist / Hans Elmlund / Ragna Peterson Wulff / Lisa Berglund / Dominika Elmlund / Cecilia Emanuelsson / Hans Hebert / Robert D Willows / Mats Hansson / Martin Lindahl / Salam Al-Karadaghi /
PubMed 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 ...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.
External links	Structure / PubMed:20223218
Methods	EM (single particle)
Resolution	7.5 - 14.0 Å
Structure data	1676 2x31 EMDB-1676: CryoEM 3D reconstruction of Rhodobacter capsulatus Mg-chelatase BchID complex in the presence of ADP PDB-2x31: Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang Method: EM (single particle) / Resolution: 7.5 Å 1677 2x31 EMDB-1677: CryoEM 3D reconstruction of Rhodobacter capsulatus Mg-chelatase BchID complex in the presence of ATP PDB-2x31: Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang Method: EM (single particle) / Resolution: 13.0 Å 1678 2x31 EMDB-1678: CryoEM 3D reconstruction of Rhodobacter capsulatus Mg-chelatase BchID complex in the presence of AMPPNP PDB-2x31: Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang Method: EM (single particle) / Resolution: 14.0 Å
Source	rhodobacter capsulatus (bacteria)
Keywords	LIGASE / BACTERIOCHLOROPHYLL BIOSYNTHESIS / PHOTOSYNTHESIS