5EUS

Rat prestin STAS domain in complex with bromide

5EUS の概要

• エントリーDOI: 10.2210/pdb5eus/pdb
• 関連するPDBエントリー: 3LLO
• 分子名称: Prestin,Rat prestin STAS domain, BROMIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: anion-binding site, protein-anion complex, transport protein
• 由来する生物種: Rattus norvegicus (Norway Rat); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q9EPH0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16289.11

構造登録者

Lolli, G.,Pasqualetto, E.,Costanzi, E.,Bonetto, G.,Battistutta, R. (登録日: 2015-11-19, 公開日: 2015-12-16, 最終更新日: 2024-01-10)

主引用文献

Lolli, G.,Pasqualetto, E.,Costanzi, E.,Bonetto, G.,Battistutta, R.
The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site.
Biochem.J., 473:365-370, 2016

PubMed Abstract: Prestin is a unique ATP- and Ca(2+)-independent molecular motor with piezoelectric characteristics responsible for the electromotile properties of mammalian cochlear outer hair cells, i.e. the capacity of these cells to modify their length in response to electric stimuli. This 'electromotility' is at the basis of the exceptional sensitivity and frequency selectivity distinctive of mammals. Prestin belongs to the SLC26 (solute carrier 26) family of anion transporters and needs anions to function properly, particularly Cl(-). In the present study, using X-ray crystallography we reveal that the STAS (sulfate transporter and anti-sigma factor antagonist) domain of mammalian prestin, considered an 'incomplete' transporter, harbours an unanticipated anion-binding site. In parallel, we present the first crystal structure of a prestin STAS domain from a non-mammalian vertebrate prestin (chicken) that behaves as a 'full' transporter. Notably, in chicken STAS, the anion-binding site is lacking because of a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin.

PubMed: 26635354
DOI: 10.1042/BJ20151089

実験手法

X-RAY DIFFRACTION (1.833 Å)