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Literature summary for 3.6.4.10 extracted from

  • Saji, H.; Iizuka, R.; Yoshida, T.; Abe, T.; Kidokoro, S.; Ishii, N.; Yohda, M.
    Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7 (2008), Proteins, 71, 771-782.
    View publication on PubMed
Search for more literature for 3.6.4.10

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
additional information construction of C-terminal truncation and amino acid replacements in the IXI/V motif leading to loss of chaperone activity of all mutants at 83°C in contrast to the wild-type enzyme, both wild type and StHsp14.0WKW exhibit almost no significant change in secondary structure at high temperatures of 85°C and 50°C. Construction of an N-terminal truncation mutants of StHsp14.0, which form stable oligomeric complexes similar to that of the wild type, but exhibits reduced chaperone activity for the protection of thermophilic IPMDH from thermal aggregation Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii
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-
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Sulfurisphaera tokodaii 7
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes by gel filtration Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Hsp14.0 exists as a spherical 24-meric oligomer showing molecular chaperone activity, e.g. to protect thermophilic 3-isopropylmalate dehydrogenase from thermal aggregation at 87°C, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles and lacks molecular chaperone activity Sulfurisphaera tokodaii ?
-
 ?
additional information Hsp14.0 exists as a spherical 24-meric oligomer showing molecular chaperone activity, e.g. to protect thermophilic 3-isopropylmalate dehydrogenase from thermal aggregation at 87°C, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles and lacks molecular chaperone activity Sulfurisphaera tokodaii 7 ?
-
 ?

Subunits

Subunits Comment Organism
More primary enzyme structures and temperature-dependent oligomeric structural changes of Hsp14.0, Hsp14.0 exists as a spherical 24-meric oligomer, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles. Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, overview Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
Hsp14.0
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 Sulfurisphaera tokodaii
Hsp19.7
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 Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 both wild type and StHsp14.0WKW exhibit almost no significant change in secondary structure at high temperatures, 85°C and 50°C Sulfurisphaera tokodaii
50
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 wild-type Hsp14.0 exhibits only slight dissociation of the oligomers at 50°C Sulfurisphaera tokodaii