5OFP

Structure of the antibacterial peptide ABC transporter McjD in an apo inward occluded conformation

5OFP の概要

• エントリーDOI: 10.2210/pdb5ofp/pdb
• 分子名称: Microcin-J25 export ATP-binding/permease protein McjD (1 entity in total)
• 機能のキーワード: abc transporter, antibacterial peptide, apo, inward occluded, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : Q9X2W0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65482.42

構造登録者

Beis, K.,Choudhury, H.G. (登録日: 2017-07-11, 公開日: 2017-09-06, 最終更新日: 2024-01-17)

主引用文献

Bountra, K.,Hagelueken, G.,Choudhury, H.G.,Corradi, V.,El Omari, K.,Wagner, A.,Mathavan, I.,Zirah, S.,Yuan Wahlgren, W.,Tieleman, D.P.,Schiemann, O.,Rebuffat, S.,Beis, K.
Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD.
EMBO J., 36:3062-3079, 2017

PubMed Abstract: Certain pathogenic bacteria produce and release toxic peptides to ensure either nutrient availability or evasion from the immune system. These peptides are also toxic to the producing bacteria that utilize dedicated ABC transporters to provide self-immunity. The ABC transporter McjD exports the antibacterial peptide MccJ25 in Our previously determined McjD structure provided some mechanistic insights into antibacterial peptide efflux. In this study, we have determined its structure in a novel conformation, apo inward-occluded and a new nucleotide-bound state, high-energy outward-occluded intermediate state, with a defined ligand binding cavity. Predictive cysteine cross-linking in membranes and PELDOR measurements along the transport cycle indicate that McjD does not undergo major conformational changes as previously proposed for multi-drug ABC exporters. Combined with transport assays and molecular dynamics simulations, we propose a novel mechanism for toxic peptide ABC exporters that only requires the transient opening of the cavity for release of the peptide. We propose that shielding of the cavity ensures that the transporter is available to export the newly synthesized peptides, preventing toxic-level build-up.

PubMed: 28864543
DOI: 10.15252/embj.201797278

実験手法

X-RAY DIFFRACTION (4.71 Å)