6WU2

Structure of the LaINDY-malate complex

Summary for 6WU2

• Entry DOI: 10.2210/pdb6wu2/pdb
• EMDB information: 21903
• Descriptor: DASS family sodium-coupled anion symporter, HEXANE, DECANE, ... (4 entities in total)
• Functional Keywords: transporter, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, membrane protein
• Biological source: Lactobacillus acidophilus
• Total number of polymer chains: 2
• Total formula weight: 114157.59

Authors

Sauer, D.B.,Marden, J.J.,Cocco, N.,Song, J.M.,Wang, D.N.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2020-05-04, release date: 2020-09-16, Last modification date: 2024-03-06)

Primary citation

Sauer, D.B.,Trebesch, N.,Marden, J.J.,Cocco, N.,Song, J.,Koide, A.,Koide, S.,Tajkhorshid, E.,Wang, D.N.
Structural basis for the reaction cycle of DASS dicarboxylate transporters.
Elife, 9:-, 2020

PubMed Abstract: Citrate, α-ketoglutarate and succinate are TCA cycle intermediates that also play essential roles in metabolic signaling and cellular regulation. These di- and tricarboxylates are imported into the cell by the divalent anion sodium symporter (DASS) family of plasma membrane transporters, which contains both cotransporters and exchangers. While DASS proteins transport substrates via an elevator mechanism, to date structures are only available for a single DASS cotransporter protein in a substrate-bound, inward-facing state. We report multiple cryo-EM and X-ray structures in four different states, including three hitherto unseen states, along with molecular dynamics simulations, of both a cotransporter and an exchanger. Comparison of these outward- and inward-facing structures reveal how the transport domain translates and rotates within the framework of the scaffold domain through the transport cycle. Additionally, we propose that DASS transporters ensure substrate coupling by a charge-compensation mechanism, and by structural changes upon substrate release.

PubMed: 32869741
DOI: 10.7554/eLife.61350

Experimental method

ELECTRON MICROSCOPY (3.36 Å)