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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.64 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

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.64 45578
-
 1 * 45578, alphabeta, sequence calculation Thermus thermophilus
3.4.24.64 47000
-
 gel filtration, recombinant enzyme Thermus thermophilus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.64 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

EC Number Subunits Comment Organism
3.4.24.64 monomer 1 * 45578, alphabeta, sequence calculation Thermus thermophilus
3.4.24.64 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

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

General Information

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