7D8I

Crystal structure of nucleoside phosphatase Sa1684 complex with ATP analogue from staphylococus aureus

7D8I の概要

• エントリーDOI: 10.2210/pdb7d8i/pdb
• 分子名称: UPF0374 protein SA1684, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: nucleotide phosphatase, cytosolic protein
• 由来する生物種: Staphylococcus aureus subsp. aureus N315
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22337.99

構造登録者

Wang, Z.,Li, X. (登録日: 2020-10-08, 公開日: 2021-03-17, 最終更新日: 2024-05-29)

主引用文献

Wang, Z.,Shen, H.,He, B.,Teng, M.,Guo, Q.,Li, X.
The structural mechanism for the nucleoside tri- and diphosphate hydrolysis activity of Ntdp from Staphylococcus aureus.
Febs J., 288:6019-6034, 2021

PubMed Abstract: Staphylococcus aureus is a well-known clinical pathogenic bacterium. In recent years, due to the emergence of multiple drug-resistant strains of S. aureus in clinical practice, S. aureus infections have become an increasingly severe clinical problem. Ntdp (nucleoside tri- and diphosphatase, also known as Sa1684) is a nucleotide phosphatase that has a significant effect on the proliferation of S. aureus colonies and the killing ability of the host. Here, we identified the nucleoside tri- and diphosphate hydrolysis activity of Ntdp and obtained the three-dimensional structures of apo-Ntdp and three substrate analog (ATP S, GDP S, and GTP S) complexes of Ntdp. Through structural analysis and biochemical verification, we illustrated the structural basis for the divalent cation selectivity, substrate recognition model, and catalytic mechanism of Ntdp. We also revealed a possible basal functional pattern of the DUF402 domain and hypothesized the potential pathways by which the protein regulates the expression of the two-component regulatory factor agr and the downstream virulence factors. Overall, the above findings provide crucial insights into our understanding of the Ntdp functional mechanism in the infection process.

PubMed: 33955674
DOI: 10.1111/febs.15911

実験手法

X-RAY DIFFRACTION (1.62 Å)