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

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

doi:10.1016/j.str.2010.01.001

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

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

Biokemi och Strukturbiologi

Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift › Peer review

Sammanfattning

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.

Originalspråk	engelska
Sidor (från-till)	354-365
Tidskrift	Structure
Volym	18
Nummer	3
DOI	https://doi.org/10.1016/j.str.2010.01.001
Status	Published - 2010

Ämnesklassifikation (UKÄ)

Biologi

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10.1016/j.str.2010.01.001

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@article{6333b7f9901e42cbbf22c759f7b5e2e2,

title = "ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.",

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 = "Joakim Lundqvist and Hans Elmlund and {Peterson Wulff}, Ragna and Lisa Berglund and Dominika Elmlund and Cecilia Emanuelsson and Hans Hebert and Willows, {Robert D} and Mats Hansson and Martin Lindahl and Salam Al-Karadaghi",

year = "2010",

doi = "10.1016/j.str.2010.01.001",

language = "English",

volume = "18",

pages = "354--365",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "3",

}

TY - JOUR

T1 - ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.

AU - Lundqvist, Joakim

AU - Elmlund, Hans

AU - Peterson Wulff, Ragna

AU - Berglund, Lisa

AU - Elmlund, Dominika

AU - Emanuelsson, Cecilia

AU - Hebert, Hans

AU - Willows, Robert D

AU - Hansson, Mats

AU - Lindahl, Martin

AU - Al-Karadaghi, Salam

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

U2 - 10.1016/j.str.2010.01.001

DO - 10.1016/j.str.2010.01.001

M3 - Article

C2 - 20223218

SN - 0969-2126

VL - 18

SP - 354

EP - 365

JO - Structure

JF - Structure

IS - 3

ER -

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

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