8G0N

FphI, Staphylococcus aureus fluorophosphonate-binding serine hydrolases I, apo form

8G0N の概要

• エントリーDOI: 10.2210/pdb8g0n/pdb
• 分子名称: Fluorophosphonate-binding serine hydrolase I, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: fphi, staphylococcus aureus, s. aureus, fluorophosphonate-binding, serine hydrolases, lipase, hydrolase
• 由来する生物種: Staphylococcus aureus USA300-0114
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27770.26

構造登録者

Fellner, M. (登録日: 2023-01-31, 公開日: 2024-02-14, 最終更新日: 2025-01-08)

主引用文献

Fellner, M.,Randall, G.,Bitac, I.R.C.G.,Warrender, A.K.,Sethi, A.,Jelinek, R.,Kass, I.
Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.
Proteins, 2024

PubMed Abstract: Staphylococcus aureus is a major cause of infections like bacteremia, pneumonia, and endocarditis. These infections are often linked to the ability of S. aureus to form biofilms. Several S. aureus serine hydrolases have previously been identified to be active during biofilm-forming conditions. Here, we present the biochemical characterization of two of these enzymes-fluorophosphonate binding hydrolase H and I (FphH, FphI). Cryogenic and room-temperature X-ray crystallography, enzymatic substrate profiling, small-angle X-ray scattering analysis, and molecular dynamics simulations provide new insights into similarities and differences between these two hydrolase_4 domain family members. We discover that these enzymes share an overall fold, including a flexible lid or cap region above the active site, which can be seen to be mobile in solution. Differences in the active site pocket and lid residues differentiate them and explain speed differences in their carboxyesterase substrate profile toward small unbranched carbon chain ester molecules. The first analysis of FphI is also compared to our previous knowledge of FphH and its association to stress conditions. These results enable the future precise targeting of Fph serine hydrolase family members with a long-term goal to significantly improve the health and wellbeing of individuals and populations worldwide.

PubMed: 39726198
DOI: 10.1002/prot.26785

実験手法

X-RAY DIFFRACTION (1.14 Å)