7KYP

PsaBC from Streptococcus pneumoniae in complex with Fab

7KYP の概要

• エントリーDOI: 10.2210/pdb7kyp/pdb
• 分子名称: Manganese ABC transporter, ATP-binding protein, Manganese ABC transporter, permease protein, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: abc transporter manganese, transport protein
• 由来する生物種: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 466501.33

構造登録者

Maher, M.J.,Sjohamn, J. (登録日: 2020-12-08, 公開日: 2021-08-25, 最終更新日: 2023-10-18)

主引用文献

Neville, S.L.,Sjohamn, J.,Watts, J.A.,MacDermott-Opeskin, H.,Fairweather, S.J.,Ganio, K.,Carey Hulyer, A.,McGrath, A.P.,Hayes, A.J.,Malcolm, T.R.,Davies, M.R.,Nomura, N.,Iwata, S.,O'Mara, M.L.,Maher, M.J.,McDevitt, C.A.
The structural basis of bacterial manganese import.
Sci Adv, 7:-, 2021

PubMed Abstract: Metal ions are essential for all forms of life. In prokaryotes, ATP-binding cassette (ABC) permeases serve as the primary import pathway for many micronutrients including the first-row transition metal manganese. However, the structural features of ionic metal transporting ABC permeases have remained undefined. Here, we present the crystal structure of the manganese transporter PsaBC from in an open-inward conformation. The type II transporter has a tightly closed transmembrane channel due to "extracellular gating" residues that prevent water permeation or ion reflux. Below these residues, the channel contains a hitherto unreported metal coordination site, which is essential for manganese translocation. Mutagenesis of the extracellular gate perturbs manganese uptake, while coordination site mutagenesis abolishes import. These structural features are highly conserved in metal-specific ABC transporters and are represented throughout the kingdoms of life. Collectively, our results define the structure of PsaBC and reveal the features required for divalent cation transport.

PubMed: 34362732
DOI: 10.1126/sciadv.abg3980

実験手法

X-RAY DIFFRACTION (2.9 Å)