3CK6

Crystal structure of ZntB cytoplasmic domain from Vibrio parahaemolyticus RIMD 2210633

「3BHC」から置き換えられました

3CK6 の概要

• エントリーDOI: 10.2210/pdb3ck6/pdb
• 分子名称: Putative membrane transport protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: apc91421.1, zntb, cytoplasmic domain, vibrio parahaemolyticus rimd 2210633, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, structural protein
• 由来する生物種: Vibrio parahaemolyticus RIMD 2210633
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 149031.98

構造登録者

Tan, K.,Sather, A.,Moy, S.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2008-03-14, 公開日: 2008-03-25, 最終更新日: 2024-10-16)

主引用文献

Tan, K.,Sather, A.,Robertson, J.L.,Moy, S.,Roux, B.,Joachimiak, A.
Structure and electrostatic property of cytoplasmic domain of ZntB transporter.
Protein Sci., 18:2043-2052, 2009

PubMed Abstract: ZntB is the distant homolog of CorA Mg(2+) transporter within the metal ion transporter superfamily. It was early reported that the ZntB from Salmonella typhimurium facilitated efflux of Zn(2+) and Cd(2+), but not Mg(2+). Here, we report the 1.90 A crystal structure of the intracellular domain of ZntB from Vibrio parahemolyticus. The domain forms a funnel-shaped homopentamer that is similar to the full-length CorA from Thermatoga maritima, but differs from two previously reported dimeric structures of truncated CorA intracellular domains. However, no Zn(2+) or Cd(2+) binding sites were identified in the high-resolution structure. Instead, 25 well-defined Cl(-) ions were observed and some of these binding sites are highly conserved within the ZntB family. Continuum electrostatics calculations suggest that the central pore of the funnel is highly attractive for cations, especially divalents. The presence of the bound Cl(-) ions increases the stability of cations along the pore suggesting they could be important in enhancing cation transport.

PubMed: 19653298
DOI: 10.1002/pro.215

実験手法

X-RAY DIFFRACTION (1.9 Å)