3DNT

structures of MDT proteins

3DNT の概要

• エントリーDOI: 10.2210/pdb3dnt/pdb
• 関連するPDBエントリー: 3DNU 3DNV 3DNW
• 分子名称: Protein hipA, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: mdt, persistence, multidrug resistance, tolerance, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101036.81

構造登録者

Schumacher, M.A. (登録日: 2008-07-02, 公開日: 2009-01-27, 最終更新日: 2024-10-30)

主引用文献

Schumacher, M.A.,Piro, K.M.,Xu, W.,Hansen, S.,Lewis, K.,Brennan, R.G.
Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB.
Science, 323:396-401, 2009

PubMed Abstract: Bacterial multidrug tolerance is largely responsible for the inability of antibiotics to eradicate infections and is caused by a small population of dormant bacteria called persisters. HipA is a critical Escherichia coli persistence factor that is normally neutralized by HipB, a transcription repressor, which also regulates hipBA expression. Here, we report multiple structures of HipA and a HipA-HipB-DNA complex. HipA has a eukaryotic serine/threonine kinase-like fold and can phosphorylate the translation factor EF-Tu, suggesting a persistence mechanism via cell stasis. The HipA-HipB-DNA structure reveals the HipB-operator binding mechanism, approximately 70 degrees DNA bending, and unexpected HipA-DNA contacts. Dimeric HipB interacts with two HipA molecules to inhibit its kinase activity through sequestration and conformational inactivation. Combined, these studies suggest mechanisms for HipA-mediated persistence and its neutralization by HipB.

PubMed: 19150849
DOI: 10.1126/science.1163806

実験手法

X-RAY DIFFRACTION (1.66 Å)