2WIU

Mercury-modified bacterial persistence regulator hipBA

2WIU の概要

• エントリーDOI: 10.2210/pdb2wiu/pdb
• 関連するPDBエントリー: 3DNT 3DNU 3DNV 3DNW
• 分子名称: PROTEIN HIPA, HTH-TYPE TRANSCRIPTIONAL REGULATOR HIPB, MERCURY (II) ION, ... (5 entities in total)
• 機能のキーワード: transferase transcription complex, serine kinase, dna-binding, mercury derivative, repressor, transcription regulation, sad, transferase-transcription complex, transferase/transcription
• 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: 122140.38

構造登録者

Evdokimov, A.,Voznesensky, I.,Fennell, K.,Anderson, M.,Smith, J.F.,Fisher, D.A. (登録日: 2009-05-17, 公開日: 2009-07-28, 最終更新日: 2024-05-08)

主引用文献

Evdokimov, A.,Voznesensky, I.,Fennell, K.,Anderson, M.,Smith, J.F.,Fisher, D.A.
New Kinase Regulation Mechanism Found in Hipba: A Bacterial Persistence Switch.
Acta Crystallogr.,Sect.D, 65:875-, 2009

PubMed Abstract: Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.

PubMed: 19622872
DOI: 10.1107/S0907444909018800

実験手法

X-RAY DIFFRACTION (2.35 Å)