6BX5
The crystal structure of fluoride channel Fluc Ec2 with Monobody S12
6BX5 の概要
| エントリーDOI | 10.2210/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 | |
| 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: 29393634DOI: 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) |
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