6QNM

Apo state of chemotaxis sensor ODP from T. denticola

6QNM の概要

• エントリーDOI: 10.2210/pdb6qnm/pdb
• 分子名称: OXYGEN-BINDING DI-IRON PROTEIN (2 entities in total)
• 機能のキーワード: chemotaxis sensor, diiron-peroxo adduct, phosphatase, signaling protein
• 由来する生物種: Treponema denticola ATCC 35404
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57798.23

構造登録者

Muok, A.R.,Chong, J.E.,Crane, B.R. (登録日: 2019-02-11, 公開日: 2019-06-19, 最終更新日: 2024-06-19)

主引用文献

Muok, A.R.,Deng, Y.,Gumerov, V.M.,Chong, J.E.,DeRosa, J.R.,Kurniyati, K.,Coleman, R.E.,Lancaster, K.M.,Li, C.,Zhulin, I.B.,Crane, B.R.
A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species.
Proc.Natl.Acad.Sci.USA, 116:14955-14960, 2019

PubMed Abstract: Many bacteria contain cytoplasmic chemoreceptors that lack sensor domains. Here, we demonstrate that such cytoplasmic receptors found in 8 different bacterial and archaeal phyla genetically couple to metalloproteins related to β-lactamases and nitric oxide reductases. We show that this oxygen-binding di-iron protein (ODP) acts as a sensor for chemotactic responses to both iron and oxygen in the human pathogen (). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable μ-peroxo adduct. Crystal structures of ODP from and the thermophile () in the Fe[III]-O, Zn[II], and apo states display differences in subunit association, conformation, and metal coordination that indicate potential mechanisms for sensing. In reconstituted systems, iron-peroxo ODP destabilizes the phosphorylated form of the receptor-coupled histidine kinase CheA, thereby providing a biochemical link between oxygen sensing and chemotaxis in diverse prokaryotes, including anaerobes of ancient origin.

PubMed: 31270241
DOI: 10.1073/pnas.1904234116

実験手法

X-RAY DIFFRACTION (2.1 Å)