6QRQ

Apo conformation of chemotaxis sensor ODP

Summary for 6QRQ

• Entry DOI: 10.2210/pdb6qrq/pdb
• Descriptor: Oxygen-binding diiron protein (2 entities in total)
• Functional Keywords: chemotaxis sensor, diiron-peroxo adduct, phosphatase, signaling protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 4
• Total formula weight: 116802.80

Authors

Muok, A.R.,Crane, B.R. (deposition date: 2019-02-19, release date: 2019-06-19, Last modification date: 2024-06-19)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.562 Å)