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3WU5

Reduced E.coli Lon Proteolytic domain

Summary for 3WU5
Entry DOI10.2210/pdb3wu5/pdb
Related3WU3 3WU4 3WU6
DescriptorLon protease, SULFATE ION (3 entities in total)
Functional Keywordsreduced form, lon protease, catalytic dyad ser-lys, hydrolase, atp binding
Biological sourceEscherichia coli
Total number of polymer chains6
Total formula weight128679.32
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: 2023-11-08)
Primary citationNishii, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.07 Å)
Structure validation

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