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8QSR

Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward-facing conformation

8QSR の概要
エントリーDOI10.2210/pdb8qsr/pdb
EMDBエントリー18640
分子名称PTS system glucose-specific EIICB component, beta-D-glucopyranose (2 entities in total)
機能のキーワードglucose transport protein, membrane protein, transport protein
由来する生物種Escherichia coli
タンパク質・核酸の鎖数2
化学式量合計107242.67
構造登録者
Roth, P.,Fotiadis, D.,Jeckelmann, J.-M. (登録日: 2023-10-11, 公開日: 2024-09-25, 最終更新日: 2025-01-22)
主引用文献Roth, P.,Jeckelmann, J.M.,Fender, I.,Ucurum, Z.,Lemmin, T.,Fotiadis, D.
Structure and mechanism of a phosphotransferase system glucose transporter.
Nat Commun, 15:7992-7992, 2024
Cited by
PubMed Abstract: Glucose is the primary source of energy for many organisms and is efficiently taken up by bacteria through a dedicated transport system that exhibits high specificity. In Escherichia coli, the glucose-specific transporter IICB serves as the major glucose transporter and functions as a component of the phosphoenolpyruvate-dependent phosphotransferase system. Here, we report cryo-electron microscopy (cryo-EM) structures of the glucose-bound IICB protein. The dimeric transporter embedded in lipid nanodiscs was captured in the occluded, inward- and occluded, outward-facing conformations. Together with biochemical and biophysical analyses, and molecular dynamics (MD) simulations, we provide insights into the molecular basis and dynamics for substrate recognition and binding, including the gates regulating the binding sites and their accessibility. By combination of these findings, we present a mechanism for glucose transport across the plasma membrane. Overall, this work provides molecular insights into the structure, dynamics, and mechanism of the IICB transporter in a native-like lipid environment.
PubMed: 39266522
DOI: 10.1038/s41467-024-52100-3
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.56 Å)
構造検証レポート
Validation report summary of 8qsr
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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