3WU6

Oxidized E.coli Lon Proteolytic domain

Summary for 3WU6

• Entry DOI: 10.2210/pdb3wu6/pdb
• Related: 3WU3 3WU4 3WU5
• Descriptor: Lon protease, SULFATE ION (3 entities in total)
• Functional Keywords: oxidized form, lon protease, catalytic dyad ser-lys, hydrolase, atp binding
• Biological source: Escherichia coli
• Total number of polymer chains: 6
• Total formula weight: 128679.32

Authors

Nishii, W.,Kukimoto-Niino, M.,Terada, T.,Shirouzu, M.,Muramatsu, T.,Yokoyama, S. (deposition date: 2014-04-22, release date: 2014-11-12, Last modification date: 2024-11-20)

Primary citation

Nishii, W.,Kukimoto-Niino, M.,Terada, T.,Shirouzu, M.,Muramatsu, T.,Kojima, M.,Kihara, H.,Yokoyama, S.
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
Nat. Chem. Biol., 11:46-51, 2015

PubMed Abstract: The Lon AAA+ protease degrades damaged or misfolded proteins in its intramolecular chamber. Its activity must be precisely controlled, but the mechanism by which Lon is regulated in response to different environments is not known. Facultative anaerobes in the Enterobacteriaceae family, mostly symbionts and pathogens, encounter both anaerobic and aerobic environments inside and outside the host's body, respectively. The bacteria characteristically have two cysteine residues on the Lon protease (P) domain surface that unusually form a disulfide bond. Here we show that the cysteine residues act as a redox switch of Lon. Upon disulfide bond reduction, the exit pore of the P-domain ring narrows by ∼30%, thus interrupting product passage and decreasing activity by 80%; disulfide bonding by oxidation restores the pore size and activity. The redox switch (E°' = -227 mV) is appropriately tuned to respond to variation between anaerobic and aerobic conditions, thus optimizing the cellular proteolysis level for each environment.

PubMed: 25383757
DOI: 10.1038/nchembio.1688

Experimental method

X-RAY DIFFRACTION (1.8 Å)