PDBsum entry 5da0

Transport protein

PDB id: 5da0

Contents

Protein chains

467 a.a.

112 a.a.

Ligands

DMU ×2

PDB id:

5da0

Name:

Transport protein

Title:

Structure of the the slc26 transporter slc26dg in complex with a nanobody

Structure:

Sulphate transporter. Chain: a. Engineered: yes. Nanobody. Chain: b. Engineered: yes

Source:

Deinococcus geothermalis (strain dsm 11300). Organism_taxid: 319795. Gene: dgeo_2773. Expressed in: escherichia coli. Expression_system_taxid: 562. Lama glama. Llama. Organism_taxid: 9844. Expression_system_taxid: 562

Resolution:

3.20Å R-factor: 0.261 R-free: 0.308

Authors:

R.Dutzler,E.R.Geertsma,Y.Chang,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:

19-Aug-15 Release date: 09-Sep-15

Protein chain

Q1J2S8  (Q1J2S8_DEIGD) -  Sulphate transporter from Deinococcus geothermalis (strain DSM 11300 / CIP 105573 / AG-3a)

Seq: 499 a.a.

Struc: 467 a.a.

Protein chain

No UniProt id for this chain

Struc: 112 a.a.

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.