8G01

YES Complex - E. coli MraY, Protein E ID21, E. coli SlyD

8G01 の概要

• エントリーDOI: 10.2210/pdb8g01/pdb
• EMDBエントリー: 29641 29642
• 分子名称: Phospho-N-acetylmuramoyl-pentapeptide-transferase, GPE, FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (3 entities in total)
• 機能のキーワード: inhibitor, antibiotic, chaperone, membrane, bacteriophage, transferase-isomerase complex, transferase/isomerase
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 132117.06

構造登録者

Orta, A.K.,Clemons, W.M.,Riera, N. (登録日: 2023-01-31, 公開日: 2023-07-26, 最終更新日: 2024-06-19)

主引用文献

Orta, A.K.,Riera, N.,Li, Y.E.,Tanaka, S.,Yun, H.G.,Klaic, L.,Clemons Jr., W.M.
The mechanism of the phage-encoded protein antibiotic from Phi X174.
Science, 381:eadg9091-eadg9091, 2023

PubMed Abstract: The historically important phage ΦX174 kills its host bacteria by encoding a 91-residue protein antibiotic called protein E. Using single-particle electron cryo-microscopy, we demonstrate that protein E bridges two bacterial proteins to form the transmembrane YES complex [MraY, protein E, sensitivity to lysis D (SlyD)]. Protein E inhibits peptidoglycan biosynthesis by obstructing the MraY active site leading to loss of lipid I production. We experimentally validate this result for two different viral species, providing a clear model for bacterial lysis and unifying previous experimental data. Additionally, we characterize the MraY structure-revealing features of this essential enzyme-and the structure of the chaperone SlyD bound to a protein. Our structures provide insights into the mechanism of phage-mediated lysis and for structure-based design of phage therapeutics.

PubMed: 37440661
DOI: 10.1126/science.adg9091

実験手法

ELECTRON MICROSCOPY (3.4 Å)