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Literature summary for 3.4.21.107 extracted from

  • Krojer, T.; Sawa, J.; Schaefer, E.; Saibil, H.R.; Ehrmann, M.; Clausen, T.
    Structural basis for the regulated protease and chaperone function of DegP (2008), Nature, 453, 885-890.
    View publication on PubMed
Search for more literature for 3.4.21.107

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the DegP24 multimer-outer membrane protein complex is solved by the single-wavelength anomalous dispersion method: The 24-mer of DegP forms a spherical shell with 432 symmetry. In the crystal structure of DegP24, eight trimers are located at the vertices of an octahedron that assembles a protein shell of about 31 A thickness enclosing a large internal cavity about 110 A in diameter Escherichia coli

Protein Variants

Protein Variants Comment Organism
K305A/K379A/K381A/K416A to monitor directly the influence of the PDZ domains on lipid binding, mutants in which the surface-exposed lysine residues are replaced by alanine: Dose-response experiments reveal that the lipid affinity of the DegP 24-mer mutant is significantly decreased. Thus DegP could function as a periplasmic macropore, allowing the protected diffusion of outer-membrane protein precursors from the inner membrane to the outer membrane Escherichia coli
K379E/K381E/K416E to monitor directly the influence of the PDZ domains on lipid binding, mutants in which the surface-exposed lysine residues are replaced by glutamate alanine: Dose-response experiments reveal that the lipid affinity of the DegP 24-mer mutant is almost entirely impaired. Thus DegP could function as a periplasmic macropore, allowing the protected diffusion of outer-membrane protein precursors from the inner membrane to the outer membrane Escherichia coli
additional information in degP-null mutant strains the levels of outer-membrane protein A, outer-membrane protein F and to smaller extent also outer-membrane protein C are decreased, indicating an active role of DegP in the outer-membrane protein biogenesis Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
LamB + H2O Escherichia coli DegP functions as a geniune chaperone ?
-
 ?
outer membrane protein A + H2O Escherichia coli in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone ?
-
 ?
outer membrane protein C + H2O Escherichia coli in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone ?
-
 ?
outer membrane protein F + H2O Escherichia coli in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0C0V0
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
LamB + H2O DegP functions as a geniune chaperone Escherichia coli ?
-
 ?
outer membrane protein A + H2O in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone Escherichia coli ?
-
 ?
outer membrane protein C + H2O in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone Escherichia coli ?
-
 ?
outer membrane protein F + H2O in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer crystal structures suggest that HtrA proteins differ in their molecular architecture, ranging from trimers with surface-accessible active sites to hexamers Escherichia coli
multimer gel filtration shows three DegP oligomers, namely the 6-mer (DegP6), the 12-mer (DegP12) and the 24-mer (DegP24), of which the two larger particles had additional proteins bound. Binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles reveal that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions Escherichia coli
trimer crystal structures suggest that HtrA proteins differ in their molecular architecture, ranging from trimers with surface-accessible active sites to hexamers Escherichia coli

Synonyms

Synonyms Comment Organism
DegP
-
 Escherichia coli
HtrA
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 Escherichia coli