6LV0

Crystal structure of the soluble domain of the multiple peptide resistance factor (MprF) from Rhizobium tropici

6LV0 の概要

• エントリーDOI: 10.2210/pdb6lv0/pdb
• 分子名称: Low pH-inducible protein LpiA (2 entities in total)
• 機能のキーワード: lipid biosynthesis, biosynthetic protein
• 由来する生物種: Rhizobium tropici CIAT 899
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74261.07

構造登録者

Jiao, H.Z.,Song, D.F.,Liu, Z.F. (登録日: 2020-02-02, 公開日: 2021-02-03, 最終更新日: 2024-03-27)

主引用文献

Song, D.,Jiao, H.,Liu, Z.
Phospholipid translocation captured in a bifunctional membrane protein MprF.
Nat Commun, 12:2927-2927, 2021

PubMed Abstract: As a large family of membrane proteins crucial for bacterial physiology and virulence, the Multiple Peptide Resistance Factors (MprFs) utilize two separate domains to synthesize and translocate aminoacyl phospholipids to the outer leaflets of bacterial membranes. The function of MprFs enables Staphylococcus aureus and other pathogenic bacteria to acquire resistance to daptomycin and cationic antimicrobial peptides. Here we present cryo-electron microscopy structures of MprF homodimer from Rhizobium tropici (RtMprF) at two different states in complex with lysyl-phosphatidylglycerol (LysPG). RtMprF contains a membrane-embedded lipid-flippase domain with two deep cavities opening toward the inner and outer leaflets of the membrane respectively. Intriguingly, a hook-shaped LysPG molecule is trapped inside the inner cavity with its head group bent toward the outer cavity which hosts a second phospholipid-binding site. Moreover, RtMprF exhibits multiple conformational states with the synthase domain adopting distinct positions relative to the flippase domain. Our results provide a detailed framework for understanding the mechanisms of MprF-mediated modification and translocation of phospholipids.

PubMed: 34006869
DOI: 10.1038/s41467-021-23248-z

実験手法

X-RAY DIFFRACTION (1.998 Å)