6N01

Structure of apo AztD from Citrobacter koseri

6N01 の概要

• エントリーDOI: 10.2210/pdb6n01/pdb
• 分子名称: AztD Protein, TRIETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: periplasm, beta propeller, zinc, metallochaperone, chaperone
• 由来する生物種: Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 182489.20

構造登録者

Yukl, E.T.,Neupane, D.P. (登録日: 2018-11-06, 公開日: 2019-09-18, 最終更新日: 2024-10-30)

主引用文献

Neupane, D.P.,Fullam, S.H.,Chacon, K.N.,Yukl, E.T.
Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.
Commun Biol, 2:308-308, 2019

PubMed Abstract: Zinc acquisition from limited environments is critical for bacterial survival and pathogenesis. AztD has been identified as a periplasmic or cell surface zinc-binding protein in numerous bacterial species. In , AztD can transfer zinc directly to AztC, the solute binding protein for a zinc-specific ATP-binding cassette transporter system, suggesting a role in zinc acquisition and homeostasis. Here, we present the first cry stal structures of AztD from and tbe human pathogen , revealing a beta-propeller fold and two high-affinity zinc-binding sites that are highly conserved among AztD homologs. These structures combined with transfer assays using WT and mutant proteins provide rare insight into the mechanism of direct zinc transfer from one protein to another. Given the importance of zinc import to bacterial pathogenesis, these insights may prove valuable to the development of zinc transfer inhibitors as antibiotics.

PubMed: 31428696
DOI: 10.1038/s42003-019-0542-z

実験手法

X-RAY DIFFRACTION (1.98 Å)