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6BX5

The crystal structure of fluoride channel Fluc Ec2 with Monobody S12

6BX5 の概要
エントリーDOI10.2210/pdb6bx5/pdb
分子名称Putative fluoride ion transporter CrcB, Monobody S12, FLUORIDE ION, ... (5 entities in total)
機能のキーワードfluc, fluoride channel, monobody, transport protein
由来する生物種Escherichia coli
詳細
タンパク質・核酸の鎖数4
化学式量合計47848.33
構造登録者
Turman, D.L.,Miller, C. (登録日: 2017-12-17, 公開日: 2018-02-14, 最終更新日: 2023-10-04)
主引用文献Turman, D.L.,Cheloff, A.Z.,Corrado, A.D.,Nathanson, J.T.,Miller, C.
Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers.
Biochemistry, 57:1212-1218, 2018
Cited by
PubMed Abstract: Fluoride ion channels of the Fluc family selectively export F ions to rescue unicellular organisms from acute F toxicity. Crystal structures of bacterial Fluc channels in complex with synthetic monobodies, fibronectin-derived soluble β-sandwich fold proteins, show 2-fold symmetric homodimers with an antiparallel transmembrane topology. Monobodies also block Fluc F current via a pore blocking mechanism. However, little is known about the energetic contributions of individual monobody residues to the affinity of the monobody-channel complex or whether the structural paratope corresponds to functional reality. This study seeks to structurally identify and compare residues interacting with Fluc between two highly similar monobodies and subjects them to mutagenesis and functional measurements of equilibrium affinities via a fluorescence anisotropy binding assay to determine their energetic contributions. The results indicate that the functional and structural paratopes strongly agree and that many Tyr residues at the interface, while playing a key role in affinity, can be substituted with Phe and Trp without large disruptions.
PubMed: 29393634
DOI: 10.1021/acs.biochem.7b01272
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 6bx5
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2026-04-22に公開中

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