Dataset Information

Cryo-EM structure of the wild-type solitary ECF module in MSP2N2 lipid nanodiscs in the ATPase open and nucleotide-free conformation (200 kV)

ABSTRACT:

SUBMITTER: Cristina Paulino

PROVIDER: EMPIAR-11309 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Expulsion mechanism of the substrate-translocating subunit in ECF transporters.

Thangaratnarajah Chancievan C Nijland Mark M Borges-Araújo Luís L Jeucken Aike A Rheinberger Jan J Marrink Siewert J SJ Souza Paulo C T PCT Paulino Cristina C Slotboom Dirk J DJ

Nature communications 20230725 1

Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogeni ...[more]

PMID: 37491368

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Project description:During evolution, chloroplasts, which originated by endosymbiosis of a prokaryotic ancestor of today's cyanobacteria with a eukaryotic host cell, were established as the site for photosynthesis. Therefore, chloroplast organelles are loaded with transition metals including iron, copper, and manganese, which are essential for photosynthetic electron transport due to their redox capacity. Although transport, storage, and cofactor-assembly of metal ions in chloroplasts are tightly controlled and crucial throughout plant growth and development, knowledge on the molecular nature of chloroplast metal-transport proteins is still fragmentary. Here, we characterized the soluble, ATP-binding ABC-transporter subunits ABCI10 and ABCI11 in Arabidopsis thaliana, which show similarities to components of prokaryotic, multisubunit ABC transporters. Both ABCI10 and ABCI11 proteins appear to be strongly attached to chloroplast-intrinsic membranes, most likely inner envelopes for ABCI10 and possibly plastoglobuli for ABCI11. Loss of ABCI10 and ABCI11 gene products in Arabidopsis leads to extremely dwarfed, albino plants showing impaired chloroplast biogenesis and deregulated metal homeostasis. Further, we identified the membrane-intrinsic protein ABCI12 as potential interaction partner for ABCI10 in the inner envelope. Our results suggest that ABCI12 inserts into the chloroplast inner envelope membrane most likely with five predicted ?-helical transmembrane domains and represents the membrane-intrinsic subunit of a prokaryotic-type, energy-coupling factor (ECF) ABC-transporter complex. In bacteria, these multisubunit ECF importers are widely distributed for the uptake of nickel and cobalt metal ions as well as for import of vitamins and several other metabolites. Therefore, we propose that ABCI10 (as the ATPase A-subunit) and ABCI12 (as the membrane-intrinsic, energy-coupling T-subunit) are part of a novel, chloroplast envelope-localized, AAT energy-coupling module of a prokaryotic-type ECF transporter, most likely involved in metal ion uptake.

Dataset Information

Cryo-EM structure of the wild-type solitary ECF module in MSP2N2 lipid nanodiscs in the ATPase open and nucleotide-free conformation (200 kV)

Publications

Expulsion mechanism of the substrate-translocating subunit in ECF transporters.

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