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Literature summary for 5.2.1.8 extracted from
- Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization (2013), J. Biol. Chem., 288, 25826-25837.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 LysY | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| FK506 | binds at the catalytic domain | Saccharomyces cerevisiae |  |
| Rapamycin | binds at the catalytic domain | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Saccharomyces cerevisiae | Fpr4 mediates cis-trans conversion of proline residues within histone tails, Pro16 and Pro30 of histone H3 are the major proline targets of Fpr4, with little activity against Pro38, mechanistic importance of substrate residues C-terminal to the peptidylprolyl bond | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21 LysY by nickel affinity chromatography, and removal of the His6 tag through tobacco etch virus protease followed by Ni2-affinity chromatography, retaining an N-terminal Gly-Ala-Met-Ala- before Lys280, followed by ultrafiltration | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Fpr4 mediates cis-trans conversion of proline residues within histone tails, Pro16 and Pro30 of histone H3 are the major proline targets of Fpr4, with little activity against Pro38, mechanistic importance of substrate residues C-terminal to the peptidylprolyl bond | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | proline isomerization of histone peptides by Fpr4(280-392) | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | solution structure of the Fpr4 C-terminal PPIase domain by NMR spectroscopy, structure calculation, overview | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| peptidyl-prolyl isomerase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases, PPIases, which share a canonical domain fold consisting of a beta-sheet composed of four large and two small -strands, opposed by a single main alpha-helix | Saccharomyces cerevisiae |
| additional information | the canonical FKBP catalytic domain actively increases the rate of isomerization of three decapeptides derived from the N-terminus of yeast histone H3, whereas maintaining intrinsic cis and trans populations. A notable feature of the FKBP catalytic domain is a prominent hydrophobic pocket that is thought to bind the proline. Specifically, Trp345 lies at the bottom of the hydrophobic pocket, with the additional residues Tyr313, Phe323, Phe332, Phe334, Val341, Ile342, Tyr368, and Phe384 forming the sides of the proline-binding cavity. The final residue, Asp324, provides a contrast to the largely hydrophic nature of the cavity. Asp324 along with the less-conserved Glu340 together comprise a small acidic region at the side of the hydrophobic pocket in Fpr4 that is otherwise surrounded by a large surface region enriched in positively charged amino acids | Saccharomyces cerevisiae |
| physiological function | Fpr4 has been described as a histone chaperone, and is implicated in epigenetic function in part due to its mediation of cis-trans conversion of proline residues within histone tails | Saccharomyces cerevisiae |
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