5IOF
Structure of the transmembrane domain of the transporter SLC26Dg
5IOF の概要
| エントリーDOI | 10.2210/pdb5iof/pdb |
| 関連するPDBエントリー | 5DA0 |
| 分子名称 | Sulphate transporter (1 entity in total) |
| 機能のキーワード | slc26 family, fumarate transporter, secondary active transport, transport protein |
| 由来する生物種 | Deinococcus geothermalis (strain DSM 11300) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 170290.36 |
| 構造登録者 | |
| 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 Cited by 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: 26367249DOI: 10.1038/nsmb.3091 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (4.2 Å) |
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