1H9S

Molybdate bound complex of Dimop domain of ModE from E.coli

1H9S の概要

• エントリーDOI: 10.2210/pdb1h9s/pdb
• 関連するPDBエントリー: 1B9M 1B9N 1H9R
• 分子名称: MOLYBDENUM TRANSPORT PROTEIN MODE, MOLYBDATE ION, ... (4 entities in total)
• 機能のキーワード: transcription regulator
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Cytoplasm: P46930 P46930
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30418.67

構造登録者

Gourley, D.G.,Hunter, W.N. (登録日: 2001-03-19, 公開日: 2001-06-19, 最終更新日: 2023-12-13)

主引用文献

Gourley, D.G.,Schuttelkopf, A.W.,Anderson, L.A.,Price, N.C.,Boxer, D.H.,Hunter, W.N.
Oxyanion Binding Alters Conformational and Quaternary Structure of the C-Terminal Domain of the Transcriptional Regulator Mode; Implications for Molybdate-Dependant Regulation, Signalling, Storage and Transport
J.Biol.Chem., 276:20641-, 2001

PubMed Abstract: The molybdate-dependent transcriptional regulator ModE of Escherichia coli functions as a sensor of intracellular molybdate concentration and a regulator for the transcription of several operons that control the uptake and utilization of molybdenum. We present two high-resolution crystal structures of the C-terminal oxyanion-binding domain in complex with molybdate and tungstate. The ligands bind between subunits at the dimerization interface, and analysis reveals that oxyanion selectivity is determined primarily by size. The relevance of the structures is indicated by fluorescence measurements, which show that the oxyanion binding properties of the C-terminal domain of ModE are similar to those of the full-length protein. Comparisons with the apoprotein structure have identified structural rearrangements that occur on binding oxyanion. This molybdate-dependent conformational switch promotes a change in shape and alterations to the surface of the protein and may provide the signal for recruitment of other proteins to construct the machinery for transcription. Sequence and structure-based comparisons lead to a classification of molybdate-binding proteins.

PubMed: 11259434
DOI: 10.1074/JBC.M100919200

実験手法

X-RAY DIFFRACTION (1.82 Å)