5DA4

Structure of a nanobody recognizing the fumarate transporter SLC26Dg

5DA4 の概要

• エントリーDOI: 10.2210/pdb5da4/pdb
• 分子名称: Nanobody recognizing the membrane protein SLC26Dg (2 entities in total)
• 機能のキーワード: membrane transport protein, nanobody complex, immune system
• 由来する生物種: Lama glama (Llama)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39913.78

構造登録者

Dutzler, R.,Geertsma, E.R.,Chang, Y.,Shaik, F.R. (登録日: 2015-08-19, 公開日: 2015-09-09, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)