8H58
Crystal structure of YhaJ effector binding domain
8H58 の概要
エントリーDOI | 10.2210/pdb8h58/pdb |
分子名称 | HTH-type transcriptional regulator YhaJ, SODIUM ION (3 entities in total) |
機能のキーワード | transcription |
由来する生物種 | Escherichia coli K-12 |
タンパク質・核酸の鎖数 | 16 |
化学式量合計 | 370324.35 |
構造登録者 | |
主引用文献 | Kim, M.,Kang, R.,Jeon, T.J.,Ryu, S.E. Structural basis of transcription factor YhaJ for DNT detection. Iscience, 26:107984-107984, 2023 Cited by PubMed Abstract: Detection of landmines without harming personnel is a global issue. The bacterial transcription factor YhaJ selectively detects metabolites of explosives, and it can be used as a key component of DNT biosensors. However, the wild-type YhaJ has a binding affinity that is not sufficient for the detection of trace amounts of explosives leaked from landmines buried in the soil. Here, we report crystal structures of the effector-binding domain of YhaJ in both the apo- and effector-bound forms. A structural comparison of the two forms revealed that the loop above the primary effector-binding site significantly switches its conformation upon effector binding. The primary effector-binding site involves hydrophobic and polar interactions, having specificity to hydroxyl-substituted benzene compounds. The structures explain the mechanism of activity-enhancing mutations and provide information for the rational engineering of YhaJ biosensors for the sensitive detection of explosives. PubMed: 37822509DOI: 10.1016/j.isci.2023.107984 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.639 Å) |
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