8JJA

SP1746 in complex with acetate ions

8JJA の概要

• エントリーDOI: 10.2210/pdb8jja/pdb
• 分子名称: bis(5'-nucleosyl)-tetraphosphatase (symmetrical), FE (III) ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: enzyme, hydrolase, hd domain superfamily protein, phosphohydrolase, unknown gene product, sp1746
• 由来する生物種: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25281.01

構造登録者

Jin, Y.,Niu, L.,Ke, J. (登録日: 2023-05-30, 公開日: 2024-05-08, 最終更新日: 2024-08-21)

主引用文献

Jin, Y.,Ke, J.,Zheng, P.,Zhang, H.,Zhu, Z.,Niu, L.
Structural and biochemical characterization of a nucleotide hydrolase from Streptococcus pneumonia.
Structure, 32:1197-1207.e4, 2024

PubMed Abstract: In this report, we structurally and biochemically characterized the unknown gene product SP1746 from Streptococcus pneumoniae serotype 4. Various crystal structures of SP1746 in the apo form and in complex with different nucleotides were determined. SP1746 is a globular protein, which belongs to the histidine-aspartate (HD) domain superfamily with two Fe ions in the active site that are coordinated by key active site residues and water molecules. All nucleotides bind in a similar orientation in the active site with their phosphate groups anchored to the diiron cluster. Biochemically, SP1746 hydrolyzes different nucleotide substrates. SP1746 most effectively hydrolyzes diadenosine tetraphosphate (Ap4A) to two ADPs. Based on the aforementioned data, we annotated SP1746 as an Ap4A hydrolase, belonging to the YqeK family. Our in vitro data indicate a potential role for SP1746 in regulating Ap4A homeostasis, which requires validation with in vivo experiments in bacteria in the future.

PubMed: 38701795
DOI: 10.1016/j.str.2024.04.009

実験手法

X-RAY DIFFRACTION (1.6 Å)