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Literature summary for 3.4.24.64 extracted from

  • Ohtsuka, J.; Ichihara, Y.; Ebihara, A.; Nagata, K.; Tanokura, M.
    Crystal structure of TTHA1264, a putative M16-family zinc peptidase from Thermus thermophilus HB8 that is homologous to the β subunit of mitochondrial processing peptidase (2009), Proteins, 75, 774-780.
    View publication on PubMed
Search for more literature for 3.4.24.64

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons, overview, expression in Escherichia coli strain BL21(DE3) Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant SeMet-labeled enzyme, sitting-drop vapor-diffusion method, 0.001 ml of protein solution containing 22.5 mg/ml protein in 20 mM Tris-HCl (pH 8.0), 150 mM NaCl, and 1 mM DTT, are mixed with 0.001 ml of reservoir solution containing 0.15 M DL-malic acid, pH 7.0, 22% PEG 3350, X-ray diffraction structure determination and analysis at 2.29 A resolution Thermus thermophilus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Thermus thermophilus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-metallopeptidase, the betaMPP subunit contains the zinc-binding motif, HxxEHx74E, essential for peptidase activity Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45578
-
 1 * 45578, alphabeta, sequence calculation Thermus thermophilus
47000
-
 gel filtration, recombinant enzyme Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SIV0
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SIV0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant MPP from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, hydroxyapatite chromatography, and gel filtration Thermus thermophilus

Subunits

Subunits Comment Organism
monomer 1 * 45578, alphabeta, sequence calculation Thermus thermophilus
More TTHA1264 possesses two repetitive domains with a canonical fold for peptidase family M16. The betaMPP subunit contains the zinc-binding motif essential for peptidase activity, while subunit alphaMPP instead possesses a glycine-rich loop, which is proposed to be important for substrate recognition or restriction. Structure analysis, modelling, overview Thermus thermophilus

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the M16 zinc peptidase family Thermus thermophilus
TTHA1264
-
 Thermus thermophilus

General Information

General Information Comment Organism
physiological function MPP is involved in the transport of nuclear-encoded proteins from the cytosol into mitochondria Thermus thermophilus