5WK0

Crystal structure of the bacillithiol transferase BstA from Staphylococcus aureus.

5WK0 の概要

• エントリーDOI: 10.2210/pdb5wk0/pdb
• 分子名称: Damage-inducible protein DinB, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: bacillithiol, detoxification, helix bundle, metalloenzyme, unknown function
• 由来する生物種: Staphylococcus sp. HMSC055H04
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18731.99

構造登録者

Cook, P.D.,Francis, J.W. (登録日: 2017-07-24, 公開日: 2018-02-21, 最終更新日: 2023-10-04)

主引用文献

Francis, J.W.,Royer, C.J.,Cook, P.D.
Structure and function of the bacillithiol-S-transferase BstA from Staphylococcus aureus.
Protein Sci., 27:898-902, 2018

PubMed Abstract: Bacillithiol is a low-molecular weight thiol produced by many gram-positive organisms, including Staphylococcus aureus and Bacillus anthracis. It is the major thiol responsible for maintaining redox homeostasis and cellular detoxification, including inactivation of the antibiotic fosfomycin. The metal-dependent bacillithiol transferase BstA is likely involved in these sorts of detoxification processes, but the exact substrates and enzyme mechanism have not been identified. Here we report the 1.34 Å resolution X-ray crystallographic structure of BstA from S. aureus. Our structure confirms that BstA belongs to the YfiT-like metal-dependent hydrolase superfamily. Like YfiT, our structure contains nickel within its active site, but our functional data suggest that BstA utilizes zinc for activity. Although BstA and YfiT both contain a core four helix bundle and coordinate their metal ions in the same fashion, significant differences between the protein structures are described here.

PubMed: 29417696
DOI: 10.1002/pro.3384

実験手法

X-RAY DIFFRACTION (1.335 Å)