5IOF

Structure of the transmembrane domain of the transporter SLC26Dg

Summary for 5IOF

• Entry DOI: 10.2210/pdb5iof/pdb
• Related: 5DA0
• Descriptor: Sulphate transporter (1 entity in total)
• Functional Keywords: slc26 family, fumarate transporter, secondary active transport, transport protein
• Biological source: Deinococcus geothermalis (strain DSM 11300)
• Total number of polymer chains: 4
• Total formula weight: 170290.36

Authors

Dutzler, R.,Geertsma, E.R.G.,Shaik, F.R. (deposition date: 2016-03-08, release date: 2016-03-16, Last modification date: 2024-01-10)

Primary citation

Geertsma, E.R.,Chang, Y.N.,Shaik, F.R.,Neldner, Y.,Pardon, E.,Steyaert, J.,Dutzler, R.
Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.
Nat. Struct. Mol. Biol., 22:803-808, 2015

PubMed Abstract: The SLC26 family of membrane proteins combines a variety of functions within a conserved molecular scaffold. Its members, besides coupled anion transporters and channels, include the motor protein Prestin, which confers electromotility to cochlear outer hair cells. To gain insight into the architecture of this protein family, we characterized the structure and function of SLC26Dg, a facilitator of proton-coupled fumarate symport, from the bacterium Deinococcus geothermalis. Its modular structure combines a transmembrane unit and a cytoplasmic STAS domain. The membrane-inserted domain consists of two intertwined inverted repeats of seven transmembrane segments each and resembles the fold of the unrelated transporter UraA. It shows an inward-facing, ligand-free conformation with a potential substrate-binding site at the interface between two helix termini at the center of the membrane. This structure defines the common framework for the diverse functional behavior of the SLC26 family.

PubMed: 26367249
DOI: 10.1038/nsmb.3091

Experimental method

X-RAY DIFFRACTION (4.2 Å)