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PDBsum entry 3wu6
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PDB id:
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Hydrolase
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Title:
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Oxidized e.Coli lon proteolytic domain
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Structure:
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Lon protease. Chain: a, b, c, d, e, f. Fragment: c-terminal proteolytic domain, unp residues 585-784. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 536056. Strain: k-12, w3110. Gene: lon, ecdh1_3170, ecdh1me8569_0424. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.80Å
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R-factor:
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0.191
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R-free:
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0.226
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Authors:
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W.Nishii,M.Kukimoto-Niino,T.Terada,M.Shirouzu,T.Muramatsu,S.Yokoyama
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Key ref:
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W.Nishii
et al.
(2015).
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
Nat Chem Biol,
11,
46-51.
PubMed id:
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Date:
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22-Apr-14
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Release date:
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12-Nov-14
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, F:
E.C.3.4.21.53
- endopeptidase La.
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Reaction:
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Hydrolysis of large proteins such as globin, casein and denaturated serum albumin, in presence of ATP.
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Nat Chem Biol
11:46-51
(2015)
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PubMed id:
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A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
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W.Nishii,
M.Kukimoto-Niino,
T.Terada,
M.Shirouzu,
T.Muramatsu,
M.Kojima,
H.Kihara,
S.Yokoyama.
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ABSTRACT
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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.
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