Literature summary extracted from
Bieniossek, C.; Niederhauser, B.; Baumann, U.M.
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation (2009), Proc. Natl. Acad. Sci. USA, 106, 21579-21584.
Activating Compound
| EC Number |
Activating Compound |
Comment |
Organism |
Structure |
|---|
| 3.4.24.B20 |
ATP |
dependent on |
Thermotoga maritima |
|
Cloned(Commentary)
| EC Number |
Cloned (Comment) |
Organism |
|---|
| 3.4.24.B20 |
expression of amino acids 147-610 of FtsH with K410L-K415A surface mutations, and expression of G404L and K207A mutants |
Thermotoga maritima |
Crystallization (Commentary)
| EC Number |
Crystallization (Comment) |
Organism |
|---|
| 3.4.24.B20 |
cytosolic region of apo-FtsH, microbatch method by mixing equal volumes of 20 mg/ml protein with crystallization buffer containing 30% w/v PEG 400, 200 mM CaCl2, 100 mM HEPES, pH 7.5, 200 mM glycine, and 0.1-0.2% w/v low-melt agarose, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution |
Thermotoga maritima |
Protein Variants
| EC Number |
Protein Variants |
Comment |
Organism |
|---|
| 3.4.24.B20 |
G404L |
site-directed mutagenesis, the mutant is monomeric and inactive in the ATPase assay and possesses only very low proteolytic activity |
Thermotoga maritima |
| 3.4.24.B20 |
K207A |
site-directed mutagenesis, crystal structure determination |
Thermotoga maritima |
Localization
| EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
|---|
| 3.4.24.B20 |
membrane |
membrane-spanning enzyme |
Thermotoga maritima |
16020 |
- |
Metals/Ions
| EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
|---|
| 3.4.24.B20 |
Zn2+ |
a metalloprotease with HEXXH motif |
Thermotoga maritima |
|
Organism
| EC Number |
Organism |
UniProt |
Comment |
Textmining |
|---|
| 3.4.24.B20 |
Thermotoga maritima |
Q9WZ49 |
- |
- |
Purification (Commentary)
| EC Number |
Purification (Comment) |
Organism |
|---|
| 3.4.24.B20 |
recombinant amino acids 147-610 of FtsH with K410L-K415A surface mutations, and recombinant G404L and K207A mutants |
Thermotoga maritima |
Substrates and Products (Substrate)
| EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
|---|
| 3.4.24.B20 |
casein + H2O |
artificial resorufin-labeled substrate |
Thermotoga maritima |
? |
- |
? |
|
| 3.4.24.B20 |
additional information |
an active-site switch is formed by a substrate-binding beta-strand |
Thermotoga maritima |
? |
- |
? |
|
Subunits
| EC Number |
Subunits |
Comment |
Organism |
|---|
| 3.4.24.B20 |
hexamer |
hexameric assembly consisting of a 6fold symmetric protease disk and a 2fold symmetric AAA ring |
Thermotoga maritima |
| 3.4.24.B20 |
More |
comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases, modelling of the apo- and ADP bound state |
Thermotoga maritima |
Synonyms
| EC Number |
Synonyms |
Comment |
Organism |
|---|
| 3.4.24.B20 |
FtsH |
- |
Thermotoga maritima |
| 3.4.24.B20 |
More |
the enzyme belongs to the AAA+ protease family |
Thermotoga maritima |
Temperature Optimum [°C]
| EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
|---|
| 3.4.24.B20 |
50 |
- |
assay at |
Thermotoga maritima |
pH Optimum
| EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
|---|
| 3.4.24.B20 |
8.8 |
- |
assay at |
Thermotoga maritima |
General Information
| EC Number |
General Information |
Comment |
Organism |
|---|
| 3.4.24.B20 |
physiological function |
FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber |
Thermotoga maritima |
