6SNR

Crystal structure of FemX

6SNR の概要

• エントリーDOI: 10.2210/pdb6snr/pdb
• 分子名称: Lipid II:glycine glycyltransferase (2 entities in total)
• 機能のキーワード: antibiotics, factors essential for meticillin resistance proteins (fem proteins), fem ligases, staphylococcus aureus, femx, enzymes involved in cross-bridge formation, antimicrobial protein
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48487.20

構造登録者

Fulop, V.,Hinxman, K. (登録日: 2019-08-27, 公開日: 2020-09-09, 最終更新日: 2024-06-19)

主引用文献

York, A.,Lloyd, A.J.,Del Genio, C.I.,Shearer, J.,Hinxman, K.J.,Fritz, K.,Fulop, V.,Dowson, C.G.,Khalid, S.,Roper, D.I.
Structure-based modeling and dynamics of MurM, a Streptococcus pneumoniae penicillin resistance determinant present at the cytoplasmic membrane.
Structure, 29:731-742.e6, 2021

PubMed Abstract: Branched Lipid II, required for the formation of indirectly crosslinked peptidoglycan, is generated by MurM, a protein essential for high-level penicillin resistance in the human pathogen Streptococcus pneumoniae. We have solved the X-ray crystal structure of Staphylococcus aureus FemX, an isofunctional homolog, and have used this as a template to generate a MurM homology model. Using this model, we perform molecular docking and molecular dynamics to examine the interaction of MurM with the phospholipid bilayer and the membrane-embedded Lipid II substrate. Our model suggests that MurM is associated with the major membrane phospholipid cardiolipin, and experimental evidence confirms that the activity of MurM is enhanced by this phospholipid and inhibited by its direct precursor phosphatidylglycerol. The spatial association of pneumococcal membrane phospholipids and their impact on MurM activity may therefore be critical to the final architecture of peptidoglycan and the expression of clinically relevant penicillin resistance in this pathogen.

PubMed: 33740396
DOI: 10.1016/j.str.2021.03.001

実験手法

X-RAY DIFFRACTION (1.62 Å)