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 (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 | Comment | Organism |
---|---|---|
S99A | does not digest peptide into smaller fragments | Helicobacter pylori |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Helicobacter pylori | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by anion exchange and gel filtration | Helicobacter pylori |
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 | Comment | Organism |
---|---|---|
ClpA | - |
Helicobacter pylori |
ClpP | - |
Helicobacter pylori |
ClpX | - |
Helicobacter pylori |