8Q4S

Crystal structure of phosphoserine phosphatase (SerB) from Brucella melitensis in complex with AP4 and magnesium.

8Q4S の概要

• エントリーDOI: 10.2210/pdb8q4s/pdb
• 分子名称: Phosphoserine phosphatase, (2S)-2-amino-4-phosphonobutanoic acid, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: complex inhibitor serine biosynthesis magnesium, hydrolase
• 由来する生物種: Brucella melitensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32941.07

構造登録者

Scaillet, T.,Wouters, J. (登録日: 2023-08-07, 公開日: 2024-08-21, 最終更新日: 2025-08-06)

主引用文献

Scaillet, T.,Pierson, E.,Fillet, M.,Wouters, J.
Structural and Enzymological Characterization of Phosphoserine Phosphatase From Brucella melitensis.
Proteins, 2025

PubMed Abstract: Amino acid L-serine (L-Ser) is a precursor of various biomolecules, including other amino acids, glutathione, and nucleotides. The metabolism of this amino acid is crucial in diseases such as brucellosis. Previous studies have revealed that the enzymes involved in L-Ser biosynthesis are essential for Brucella replication, making them potential targets for the development of new drugs. Here, we focus on Brucella melitensis phosphoserine phosphatase (BmPSP), which catalyzes the dephosphorylation of phosphoserine in L-Ser. The enzyme is characterized through enzymatic and structural studies, leading to the discovery of its first crystallographic structures. The interactions of BmPSP with different ligands are also investigated. We demonstrate that the substitution of its Mg cofactor with Ca inhibits the enzyme and results in a slight movement of catalytic residues in the active site. Crystallographic structures of BmPSP in complex with substrate, reaction products, and substrate analogs are also detailed, revealing the interaction between these molecules and the active site residues. This structural study provides a better understanding of phosphoserine phosphatases, highlighting the involvement of two highly conserved residues in the mechanism of substrate entry into the active site.

PubMed: 40719280
DOI: 10.1002/prot.70027

実験手法

X-RAY DIFFRACTION (2.08 Å)