8G4C

BceABS ATPgS high res TM

8G4C の概要

• エントリーDOI: 10.2210/pdb8g4c/pdb
• EMDBエントリー: 29690 29691 29694 29701 29716 29717
• 分子名称: Bacitracin export permease protein BceB, Bacitracin export ATP-binding protein BceA, Sensor protein BceS, ... (5 entities in total)
• 機能のキーワード: abc transporter, histidine kinase, antimicrobial, membrane protein
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 210147.15

構造登録者

George, N.L.,Orlando, B.J. (登録日: 2023-02-09, 公開日: 2023-06-21, 最終更新日: 2025-06-04)

主引用文献

George, N.L.,Orlando, B.J.
Architecture of a complete Bce-type antimicrobial peptide resistance module.
Nat Commun, 14:3896-3896, 2023

PubMed Abstract: Gram-positive bacteria synthesize and secrete antimicrobial peptides that target the essential process of peptidoglycan synthesis. These antimicrobial peptides not only regulate the dynamics of microbial communities but are also of clinical importance as exemplified by peptides such as bacitracin, vancomycin, and daptomycin. Many gram-positive species have evolved specialized antimicrobial peptide sensing and resistance machinery known as Bce modules. These modules are membrane protein complexes formed by an unusual Bce-type ABC transporter interacting with a two-component system sensor histidine kinase. In this work, we provide the first structural insight into how the membrane protein components of these modules assemble into a functional complex. A cryo-EM structure of an entire Bce module revealed an unexpected mechanism of complex assembly, and extensive structural flexibility in the sensor histidine kinase. Structures of the complex in the presence of a non-hydrolysable ATP analog reveal how nucleotide binding primes the complex for subsequent activation. Accompanying biochemical data demonstrate how the individual membrane protein components of the complex exert functional control over one another to create a tightly regulated enzymatic system.

PubMed: 37393310
DOI: 10.1038/s41467-023-39678-w

実験手法

ELECTRON MICROSCOPY (3.1 Å)