3G40

Crystal structure of the cytoplasmic domain of a prokaryotic cation chloride cotransporter

3G40 の概要

• エントリーDOI: 10.2210/pdb3g40/pdb
• 分子名称: Na-K-Cl cotransporter (2 entities in total)
• 機能のキーワード: alpha/beta fold 10-stranded twisted beta sheet, transport protein
• 由来する生物種: Methanosarcina acetivorans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33244.98

構造登録者

Warmuth, S.,Zimmermann, I.,Dutzler, R. (登録日: 2009-02-03, 公開日: 2009-04-28, 最終更新日: 2024-03-20)

主引用文献

Warmuth, S.,Zimmermann, I.,Dutzler, R.
X-ray Structure of the C-Terminal Domain of a Prokaryotic Cation-Chloride Cotransporter
Structure, 17:538-546, 2009

PubMed Abstract: The cation-chloride cotransporters (CCCs) mediate the electroneutral transport of chloride in dependence of sodium and potassium. The proteins share a conserved structural scaffold that consists of a transmembrane transport domain followed by a cytoplasmic regulatory domain. We have determined the X-ray structure of the C-terminal domain of the archaea Methanosarcina acetivorans. The structure shows a novel fold of a regulatory domain that is distantly related to universal stress proteins. The protein forms dimers in solution, which is consistent with the proposed dimeric organization of eukaryotic CCC transporters. The dimer interface observed in different crystal forms is unusual because the buried area is relatively small and hydrophilic. By using a biochemical approach we show that this interaction is preserved in solution and in the context of the full-length transporter. Our studies reveal structural insight into the CCC family and establish the oligomeric organization of this important class of transport proteins.

PubMed: 19368887
DOI: 10.1016/j.str.2009.02.009

実験手法

X-RAY DIFFRACTION (1.9 Å)