9LTK

Crystal structur of Lpg1618(R215F) from Legionella pneumophila

9LTK の概要

• エントリーDOI: 10.2210/pdb9ltk/pdb
• 分子名称: Beta-lactamase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-lactamase, oxa-29, hydrolase
• 由来する生物種: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61002.59

構造登録者

Liu, T.,Gao, J.,Ge, H. (登録日: 2025-02-06, 公開日: 2025-06-25)

主引用文献

Gao, J.,Liu, T.,Lu, L.,Zhou, Z.,Sun, W.,Chen, Y.,Xu, W.,Wang, N.,Ma, J.,Ge, H.
Structural and molecular characterization of AmpS, a class D beta-lactamase from Legionella pneumophila.
Int.J.Biol.Macromol., 312:144174-144174, 2025

PubMed Abstract: In Gram-negative bacteria, β-lactamase enzymes represent one of the most prevalent mechanisms of antibiotic resistance. These enzymes confer resistance by hydrolyzing the four-membered β-lactam ring in β-lactam antibiotics, resulting in inactive derivatives. In this study, we report the 1.9 Å crystal structure of the R215F mutant of AmpS, a class D β-lactamase OXA-29 from Legionella pneumophila. The R215F mutation was designed to mimic the phenylalanine residue present at the equivalent position in E. coli OXA-1, thereby enabling functional investigation of the surrounding region and its role in substrate specificity. Through molecular docking simulations, enzymatic activity assays, and physiological analyses, we characterized the molecular properties of AmpS and its contribution to β-lactam resistance in L. pneumophila. Our findings provide new insights into the function of AmpS, underscoring its contribution to antibiotic resistance and offering a foundation for the development of therapeutic strategies aimed at mitigating β-lactamase-mediated resistance in pathogenic bacteria such as L. pneumophila.

PubMed: 40379166
DOI: 10.1016/j.ijbiomac.2025.144174

実験手法

X-RAY DIFFRACTION (1.9 Å)