5T77

Crystal structure of the MOP flippase MurJ

5T77 の概要

• エントリーDOI: 10.2210/pdb5t77/pdb
• 分子名称: Putative lipid II flippase MurJ, CHLORIDE ION, ZINC ION, ... (9 entities in total)
• 機能のキーワード: transporter, flippase, peptidoglycan, transport protein
• 由来する生物種: Thermosipho africanus (strain TCF52B)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69166.74

構造登録者

Kuk, A.C.Y.,Lee, S.-Y. (登録日: 2016-09-02, 公開日: 2016-12-28, 最終更新日: 2024-03-06)

主引用文献

Kuk, A.C.,Mashalidis, E.H.,Lee, S.Y.
Crystal structure of the MOP flippase MurJ in an inward-facing conformation.
Nat. Struct. Mol. Biol., 24:171-176, 2017

PubMed Abstract: Peptidoglycan (PG) protects bacteria from osmotic lysis, and its biogenesis is a key antibiotic target. A central step in PG biosynthesis is flipping of the lipid-linked PG precursor lipid II across the cytoplasmic membrane for subsequent incorporation into PG. MurJ, part of the multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) transporter superfamily, was recently shown to carry out this process. However, understanding of how MurJ flips lipid II, and of how MOP transporters operate in general, remains limited due to a lack of structural information. Here we present a crystal structure of MurJ from Thermosipho africanus in an inward-facing conformation at 2.0-Å resolution. A hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Our studies not only provide the first structural glimpse of MurJ but also suggest that alternating access is important for MurJ function, which may be applicable to other MOP superfamily transporters.

PubMed: 28024149
DOI: 10.1038/nsmb.3346

実験手法

X-RAY DIFFRACTION (2 Å)