1O7L
Molybdate-activated form of ModE from Escherichia coli
1O7L の概要
エントリーDOI | 10.2210/pdb1o7l/pdb |
関連するPDBエントリー | 1B9M 1B9N 1H9R 1H9S |
分子名称 | TRANSCRIPTIONAL REGULATOR MODE, MOLYBDATE ION, CHLORIDE ION, ... (5 entities in total) |
機能のキーワード | transcription regulation, dna binding, molybdate, mop, winged helix-turn-helix, transcriptional regulator, activator |
由来する生物種 | ESCHERICHIA COLI |
細胞内の位置 | Cytoplasm: P46930 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 114107.80 |
構造登録者 | |
主引用文献 | Schuttelkopf, A.W.,Boxer, D.H.,Hunter, W.N. Crystal Structure of Activated Mode Reveals Conformational Changes Involving Both Oxyanion and DNA-Binding Domains J.Mol.Biol., 326:761-, 2003 Cited by PubMed Abstract: ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with molybdate, which was determined at 2.75A from a merohedrally twinned crystal (twin fraction approximately 0.30) with space group P4(3). We now have structures of ModE in both its "switched on" (ligand-bound) and "switched off" (apo) states. Comparison with the apo structure shows that ligand binding leads to extensive conformational changes not only in the molybdate-binding domain, but also in the DNA-binding domain. The most obvious difference is the loss of the pronounced asymmetry between the two chains of the ModE dimer, which had been a characteristic property of the apo structure. Another major change concerns the relative orientation of the two DNA-interacting winged helix-turn-helix motifs. Manual docking of an idealized DNA structure suggests that this conformational change should improve DNA binding of the activated molybdate-bound ModE. PubMed: 12581638DOI: 10.1016/S0022-2836(02)01358-X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.75 Å) |
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