PDBsum entry 5iof

Transport protein

PDB id: 5iof

Contents

Protein chains

374 a.a.

PDB id:

5iof

Name:

Transport protein

Title:

Structure of the transmembrane domain of the transporter slc26dg

Structure:

Sulphate transporter. Chain: a, b, c, d. Engineered: yes

Source:

Deinococcus geothermalis (strain dsm 11300). Organism_taxid: 319795. Strain: dsm 11300. Gene: dgeo_2773. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

4.20Å R-factor: 0.293 R-free: 0.312

Authors:

R.Dutzler,E.R.G.Geertsma,F.R.Shaik

Key ref:

E.R.Geertsma et al. (2015). Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family. Nat Struct Biol, 22, 803-808. PubMed id: 26367249 DOI: 10.1038/nsmb.3091

Date:

08-Mar-16 Release date: 16-Mar-16

Protein chains

Q1J2S8  (Q1J2S8_DEIGD) -  Sulphate transporter from Deinococcus geothermalis (strain DSM 11300 / AG-3a)

Seq: 499 a.a.

Struc: 374 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsmb.3091

Nat Struct Biol 22:803-808 (2015)

PubMed id: 26367249

Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.

E.R.Geertsma, Y.N.Chang, F.R.Shaik, Y.Neldner, E.Pardon, J.Steyaert, R.Dutzler.

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.