5YXC

Crystal structure of Zinc binding protein ZinT in complex with citrate from E. coli

5YXC の概要

• エントリーDOI: 10.2210/pdb5yxc/pdb
• 分子名称: Metal-binding protein ZinT, ZINC ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: zinc binding protein, complex, citrate, metal binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50106.80

構造登録者

Chen, J.,Wang, L.,Shang, F.,Xu, Y. (登録日: 2017-12-04, 公開日: 2017-12-20, 最終更新日: 2024-11-13)

主引用文献

Chen, J.,Wang, L.,Shang, F.,Dong, Y.,Ha, N.C.,Nam, K.H.,Quan, C.,Xu, Y.
Crystal structure of E. coli ZinT with one zinc-binding mode and complexed with citrate
Biochem. Biophys. Res. Commun., 500:139-144, 2018

PubMed Abstract: The ZnuABC ATP-binding cassette transporter found in gram-negative bacteria has been implicated in ensuring adequate zinc import into Zn(II)-poor environments. ZinT is an essential component of ZnuABC and contributes to metal transport by transferring metals to ZnuA, which delivers them to ZnuB in periplasmic zinc recruitment. Although several structures of E. coli ZinT have been reported, its zinc-binding sites and oligomeric state have not been clearly identified. Here, we report the crystal structure of E. coli ZinT at 1.76 Å resolution. This structure contains one zinc ion in its calycin-like domain, and this ion is coordinated by three highly conserved histidine residues (His167, His176 and His178). Moreover, three oxygen atoms (O, O and O) from the citrate molecule interact with zinc, giving the zinc ion stable octahedral coordination. Our EcZinT structure shows the fewest zinc ions bound of all reported EcZinT structures. Crystallographic packing and size exclusion chromatography suggest that EcZinT prefers to form monomers in solution. Our results provide insights into the molecular function of ZinT.

PubMed: 29596824
DOI: 10.1016/j.bbrc.2018.03.192

実験手法

X-RAY DIFFRACTION (1.763 Å)