8TLU

E. coli MraY mutant-T23P

8TLU の概要

• エントリーDOI: 10.2210/pdb8tlu/pdb
• EMDBエントリー: 41373
• 分子名称: Phospho-N-acetylmuramoyl-pentapeptide-transferase (1 entity in total)
• 機能のキーワード: peptidoglycan, phosphotransferase, membrane protein
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79811.10

構造登録者

Orta, A.K.,Li, Y.E.,Clemons, W.M. (登録日: 2023-07-27, 公開日: 2024-05-01)

主引用文献

Marmont, L.S.,Orta, A.K.,Baileeves, B.W.A.,Sychantha, D.,Fernandez-Galliano, A.,Li, Y.E.,Greene, N.G.,Corey, R.A.,Stansfeld, P.J.,Clemons Jr., W.M.,Bernhardt, T.G.
Synthesis of lipid-linked precursors of the bacterial cell wall is governed by a feedback control mechanism in Pseudomonas aeruginosa.
Nat Microbiol, 9:763-775, 2024

PubMed Abstract: Many bacterial surface glycans such as the peptidoglycan (PG) cell wall are built from monomeric units linked to a polyprenyl lipid carrier. How this limiting carrier is distributed among competing pathways has remained unclear. Here we describe the isolation of hyperactive variants of Pseudomonas aeruginosa MraY, the enzyme that forms the first lipid-linked PG precursor. These variants result in the elevated production of the final PG precursor lipid II in cells and are hyperactive in vitro. The activated MraY variants have substitutions that map to a cavity on the extracellular side of the dimer interface, far from the active site. Our structural and molecular dynamics results suggest that this cavity is a binding site for externalized lipid II. Overall, our results support a model in which excess externalized lipid II allosterically inhibits MraY, providing a feedback mechanism that prevents the sequestration of lipid carrier in the PG biogenesis pathway.

PubMed: 38336881
DOI: 10.1038/s41564-024-01603-2

実験手法

ELECTRON MICROSCOPY (3.8 Å)