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Literature summary for 3.4.21.53 extracted from

  • Rotanova, T.V.; Botos, I.; Melnikov, E.E.; Rasulova, F.; Gustchina, A.; Maurizi, M.R.; Wlodawer, A.
    Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains (2006), Protein Sci., 15, 1815-1828.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information activity of yeast lon alpha-proteolytic fragment enhanced when it is coexpressed with a construct containing the N- and A-domains (residues 1-917) Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
lon-N119 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
digestion of lonA by alpha-chymotrypsin yields a stable fragment consisting of residues 491-584 crystallized. Crystal structure of the proteolytic domain of lonA (residues 585-784) elucidates a unique fold, P31 space group Escherichia coli
proteolytic domain Archaeoglobus fulgidus

Protein Variants

Protein Variants Comment Organism
D676N is completely inactive for protein degradation, it retains some basal ATPase activity, but no activation of ATPase activity occurs upon binding of protein substrates Escherichia coli
E614K is a dominant-negative mutant, can form mixed oligomers with wild-type lon and interferes with its activity Escherichia coli
K362Q intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation Escherichia coli
additional information lon mutant altered in substrate specificity. A mutation in lon that converts Glu240 to Lys results in stabilization of lon substrate RcsA in vivo but does not affect the degradation of lon substrate SulA. lon lacking 107 N-terminal residues has drastically reduced protein degrading activity in vitro Escherichia coli
S679A inactive, intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation Escherichia coli
T534A retains significant proteolytic activity Archaeoglobus fulgidus
T704A retains significant proteolytic activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae construct containing residues 793-1133 of yeast lon, which comprises the proteolytic domain along with most of the alpha-domain, exhibits low but significant proteolytic activity in vivo ?
-
?

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus
-
-
-
Bordetella parapertussis
-
-
-
Brevibacillus thermoruber
-
-
-
Escherichia coli
-
-
-
Methanocaldococcus jannaschii
-
-
-
Mycolicibacterium smegmatis
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bordetella parapertussis
lon-N119 purified. Digestion of lonA by alpha-chymotrypsin yields a stable fragment consisting of residues 491-584 purified. lon proteolytic domain purified Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information construct containing residues 793-1133 of yeast lon, which comprises the proteolytic domain along with most of the alpha-domain, exhibits low but significant proteolytic activity in vivo Saccharomyces cerevisiae ?
-
?
additional information lacks 90, 225, or 277 N-terminal residues, practically no proteolytic activity while exhibiting reduced protein binding activity Mycolicibacterium smegmatis ?
-
?
additional information proteolytic domain and a a large N-terminal domain, active site has a Ser-Lys catalytic dyad. Proteolytic domain exhibits no detectable activity against protein substrates degraded by full-length lon, but retains a significant fraction of peptidase activity Escherichia coli ?
-
?
additional information proteolytic domain and a large transmembrane domain insertion within the AAA+ module between the Walker motifs A and B Archaeoglobus fulgidus ?
-
?
additional information yeast lon has a relatively poor ability to unravel proteins and is only able to degrade proteins that have unstable tertiary structure Saccharomyces cerevisiae ?
-
?
RcsA + H2O
-
Escherichia coli ?
-
?
SulA + H2O
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Mycolicibacterium smegmatis
heptamer electron microscopic image analysis Saccharomyces cerevisiae
hexamer
-
Mycolicibacterium smegmatis
hexamer crystallography Archaeoglobus fulgidus
hexamer gel filtration, sedimentation velocity experiments and cross-linking of intact and truncated species Brevibacillus thermoruber
hexamer negative stain electron microscopy, crystallography of the proteolytic domain Escherichia coli
monomer proteolytic domain in solution Escherichia coli
monomer proteolytic domain in solution Archaeoglobus fulgidus
octamer sedimentation Escherichia coli
tetramer
-
Mycolicibacterium smegmatis
tetramer sedimentation Escherichia coli
trimer
-
Mycolicibacterium smegmatis

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
Escherichia coli
ATP-dependent lon protease
-
Methanocaldococcus jannaschii
ATP-dependent lon protease
-
Archaeoglobus fulgidus
BPP1347 similarity between BPP1347 and fragments of the N-domain of lon Bordetella parapertussis
lon
-
Saccharomyces cerevisiae
lon
-
Mycolicibacterium smegmatis
lon
-
Brevibacillus thermoruber
lon protease
-
Escherichia coli
lon protease
-
Methanocaldococcus jannaschii
lon protease
-
Archaeoglobus fulgidus
lonA
-
Escherichia coli
lonB
-
Methanocaldococcus jannaschii
lonB
-
Archaeoglobus fulgidus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae
ATP ATPase domain that includes AAA+ modules Escherichia coli
ATP ATPase domain that includes AAA+ modules Archaeoglobus fulgidus