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Literature summary for 3.4.21.53 extracted from

  • Su, S.C.; Lin, C.C.; Tai, H.C.; Chang, M.Y.; Ho, M.R.; Babu, C.S.; Liao, J.H.; Wu, S.H.; Chang, Y.C.; Lim, C.; Chang, C.I.
    Structural basis for the magnesium-dependent activation and hexamerization of the Lon AAA+ protease (2016), Structure, 24, 676-686 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information magnesium-dependent activation and hexamerization of the Lon AAA+ protease Meiothermus taiwanensis

Cloned(Commentary)

Cloned (Comment) Organism
gene lonA1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Meiothermus taiwanensis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant full-length wild-type enzyme LonA in complex with bortezomib and Mg2+, and in apoform with Mg2+, hexameric and dodecameric enzyme crystals, AAAP-Mg2+-bortezomib complex by hanging drop vapor diffusion method, for the apoenzyme-Mg2+ crystals, 400 nl of 8 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, and 10 mM MgCl2, is mixed with 400 nl of well solution containing 20% PEG 3000, 0.1 M HEPES, pH 7.5, and 0.2 M NaCl, for the complex crystals, mixing of 0.001 ml of protein-inhibitor solution with 0.001 ml of well solution containing 0.2 M sodium citrate, pH 6.5, and 10% PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 1.85 A and 3.05 A resolution, respectively, molecular replacement Meiothermus taiwanensis

Protein Variants

Protein Variants Comment Organism
E423Q site-directed mutagenesis, structure determination Meiothermus taiwanensis
I398G site-directed mutagenesis Meiothermus taiwanensis
additional information generation of truncated enzyme versions, AAAP(residues 295-793) and AP(residues 492-793) Meiothermus taiwanensis
S678A site-directed mutagenesis Meiothermus taiwanensis
Y397G site-directed mutagenesis Meiothermus taiwanensis
Y397G/I398G site-directed mutagenesis, the mutant fails to degrade alpha-casein with Mg2+ and ATP. The Mg2+-activated double mutant showed wild-type-like ATP-independent proteolysis Meiothermus taiwanensis

Inhibitors

Inhibitors Comment Organism Structure
bortezomib enzyme-bound structure analysis Meiothermus taiwanensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ magnesium-dependent activation and hexamerization of the Lon AAA+ protease. Mg2+-binding site structure analysis, Mg2+ is bound in the proteolytic groove Meiothermus taiwanensis

Organism

Organism UniProt Comment Textmining
Meiothermus taiwanensis A0A059VAZ3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Meiothermus taiwanensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O
-
Meiothermus taiwanensis ?
-
?
Ig2 + H2O
-
Meiothermus taiwanensis ?
-
?

Subunits

Subunits Comment Organism
hexamer Mg2+-activated LonA forms an open hexameric chamber without nucleotide Meiothermus taiwanensis
More Mg2+-dependent activation and hexamerization of the Lon AAA+ protease. Role of the protease domains in the oligomerization and activity of LonA, overview Meiothermus taiwanensis

Synonyms

Synonyms Comment Organism
AAAP
-
Meiothermus taiwanensis
Lon AAA+ protease
-
Meiothermus taiwanensis
lonA
-
Meiothermus taiwanensis
MtaLonA
-
Meiothermus taiwanensis

Cofactor

Cofactor Comment Organism Structure
AMPPNP adenylylimidodiphosphate, is not as effective as ATP, slight activation Meiothermus taiwanensis
ATP activates Meiothermus taiwanensis
additional information Mg2+-activated LonA degrades unfolded protein or peptides without ATP Meiothermus taiwanensis

General Information

General Information Comment Organism
additional information Mg2+-activated LonA can operate as a diffusion-based chambered protease to degrade unstructured protein and peptide substrates efficiently in the absence of ATP. Mg2+-dependent remodeling of a substrate-binding loop and a potential metal-binding site near the Ser-Lys catalytic dyad, supported by biophysical binding assays and molecular dynamics simulations, domain arrangement and structural modeling, overview Meiothermus taiwanensis
physiological function the Lon AAA+ protease (LonA) plays important roles in protein homeostasis and regulation of diverse biological processes. Proposed Mg2+- and nucleotide-dependent assembly pathway of LonA, overview Meiothermus taiwanensis