Literature summary for 3.4.21.53 extracted from

Li, J.K.; Liao, J.H.; Li, H.; Kuo, C.I.; Huang, K.F.; Yang, L.W.; Wu, S.H.; Chang, C.I.
The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones (2013), Acta Crystallogr. Sect. D, 69, 1789-1797.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene lonC, cloning and expression of N-terminally His6-tagged residues 35-387 of the N-terminal domain of the mutant L91M/L188M/I359M enzyme with a TEV protease-cleavage site as selenomethionine-labeled protein in Escherichia coli strain B834(DE3)	Meiothermus taiwanensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant selenomethionine-labeled N-terminal domain mutant L91M/L188M/I359M , mixing of 0.001 ml of 8 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10% v/v glycerol, 1 mM DTT, with 0.001 ml of well solution containing consisting of 400 mM lithium sulfate, 10 mM nickel chloride, 100 mM Tris-HCl, pH 8.4, 22°C, 7 days to 3 months, Selected crystals are further dehydrated for 3 days in sitting drops equilibrated against 0.7-1.2 M lithium sulfate, X-ray diffraction structure determination and analysis at 3.1-3.4 A resolution, modelling	Meiothermus taiwanensis

Crystallization (Comment)

Organism

purified recombinant selenomethionine-labeled N-terminal domain mutant L91M/L188M/I359M , mixing of 0.001 ml of 8 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10% v/v glycerol, 1 mM DTT, with 0.001 ml of well solution containing consisting of 400 mM lithium sulfate, 10 mM nickel chloride, 100 mM Tris-HCl, pH 8.4, 22°C, 7 days to 3 months, Selected crystals are further dehydrated for 3 days in sitting drops equilibrated against 0.7-1.2 M lithium sulfate, X-ray diffraction structure determination and analysis at 3.1-3.4 A resolution, modelling

Meiothermus taiwanensis

Protein Variants

Protein Variants	Comment	Organism
L91M/L188M/I359M	site-directed mutagenesis, the three mutations are introduced into the wild-type sequence to facilitate de novo phasing	Meiothermus taiwanensis
additional information	generation of deletion mutations MtaLonCdelta (removing residues 506-511) and MtaLonCDELTAHHE (replacing residues 118-205 with a triglycine linker) by a PCR-based strategy	Meiothermus taiwanensis

Organism

Organism	UniProt	Comment	Textmining
Meiothermus taiwanensis	C9DRU9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant selenomethionine-labeled N-terminally His6-tagged N-terminal domain of mutant L91M/L188M/I359M enzyme from Escherichia coli strain B834(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, anion exchange chromatography, and gel filtration	Meiothermus taiwanensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Abz-QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A + H2O	i.e. F-beta20-Q peptide, a synthetic fluorogenic peptide	Meiothermus taiwanensis	?	-	?

Subunits

Subunits	Comment	Organism
More	quaternary enzyme structure, modelling, overview	Meiothermus taiwanensis

Synonyms

Synonyms	Comment	Organism
LonC	-	Meiothermus taiwanensis
LonC protease	-	Meiothermus taiwanensis
MtaLonC	-	Meiothermus taiwanensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
55	-	assay at	Meiothermus taiwanensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Meiothermus taiwanensis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	ATP-dependent protease, the enzyme contains an AAA-like domain that lacks the conserved ATPase motifs. The LonC AAA-like domain is inserted with a large domain predicted to be largely alpha-helical, the unique Lon-insertion domain is disordered in the full-length crystal structure of Meiothermus taiwanensis LonC	Meiothermus taiwanensis

General Information

General Information	Comment	Organism
evolution	although Lon is originally identified as an ATP-dependent protease with fused AAA+ (ATPases associated with diverse cellular activities) and protease domains, analyses have recently identified LonC as a class of Lon-like proteases with no intrinsic ATPase activity. In contrast to the canonical ATP-dependent Lon present in eukaryotic organelles and prokaryotes, LonC contains an AAA-like domain that lacks the conserved ATPase motifs	Meiothermus taiwanensis
additional information	the N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones	Meiothermus taiwanensis
physiological function	the Lon-insertion domain of LonC is involved both in Skplike chaperone activity and in recognition of unfolded protein substrates, structure of Lon-insertion domain is remarkably similar to the tentacle-like prong of the periplasmic chaperone Skp	Meiothermus taiwanensis