2CFQ
Sugar Free Lactose Permease at neutral pH
2CFQ の概要
| エントリーDOI | 10.2210/pdb2cfq/pdb |
| 関連するPDBエントリー | 1M2U 1PV6 1PV7 2CFP |
| 分子名称 | LACTOSE PERMEASE, MERCURY (II) ION (2 entities in total) |
| 機能のキーワード | transport, lactose permease, transport mechanism, lactose/h+ symport, sugar transport, transmembrane, formylation |
| 由来する生物種 | ESCHERICHIA COLI |
| 細胞内の位置 | Cell inner membrane; Multi-pass membrane protein: P02920 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 47487.75 |
| 構造登録者 | Mirza, O.,Guan, L.,Verner, G.,Iwata, S.,Kaback, H.R. (登録日: 2006-02-22, 公開日: 2006-03-13, 最終更新日: 2023-12-13) |
| 主引用文献 | Mirza, O.,Guan, L.,Verner, G.,Iwata, S.,Kaback, H.R. Structural Evidence for Induced Fit and a Mechanism for Sugar/H(+) Symport in Lacy. Embo J., 25:2038-, 2006 Cited by PubMed Abstract: Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction. PubMed: 16525509DOI: 10.1038/SJ.EMBOJ.7601028 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.95 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






