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Literature summary for 3.4.21.92 extracted from

  • Kim, D.Y.; Kim, K.K.
    The structural basis for the activation and peptide recognition of bacterial ClpP (2008), J. Mol. Biol., 379, 760-771.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the entire ClpP gene (amino acid residues 1-196) transferred into pET-22b(+) and expressed in Escherichia coli BL21(DE3) Helicobacter pylori

Crystallization (Commentary)

Crystallization (Comment) Organism
by the microbatch method at 14°C. Crystal structure of ClpP, at a resolution of 2.6 A, in complex with product peptides (heptapeptide) bound to the active site as well as in the apo state and crystal structure of the ClpP mutant, at 2.5 A resolution, and in complex with a tetrapeptide. In the complex structure, the peptides are zipped with two antiparallel strands of ClpP and point to the adjacent active site, explaining the broad substrate specificity, the product inhibition and the processive degradation of substrates in the chamber. Substrate binding causes local conformational changes around the active site that ultimately induce the active conformation of ClpP. The peptide binds to the active site of ClpP via hydrogen-bond networks Helicobacter pylori

Protein Variants

Protein Variants Comment Organism
S99A does not digest peptide into smaller fragments Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by anion exchange and gel filtration Helicobacter pylori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
-
Helicobacter pylori N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
?

Synonyms

Synonyms Comment Organism
ClpA
-
Helicobacter pylori
ClpP
-
Helicobacter pylori
ClpX
-
Helicobacter pylori