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Literature summary extracted from

  • Merski, M.; Moreira, C.; Abreu, R.M.; Ramos, M.J.; Fernandes, P.A.; Martins, L.M.; Pereira, P.J.B.; Macedo-Ribeiro, S.
    Molecular motion regulates the activity of the mitochondrial serine protease HtrA2 (2017), Cell Death Dis., 8, e3119 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.108 to 1.65 A resolution. The catalytic triad in the HtrA2 wild-type structure is disrupted, with the nearest accessible H198 side chain atom positioned 5.9 A away from the carboxylate oxygen of D228 and separated from the hydroxyl of S306 by 7.4 A, requiring substantial rearrangements to reestablish a catalytically competent conformation. Dynamic protein motions are important to HtrA protease activity Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.108 S306A presence of a serine residue in position 306 favors an inactive conformation of H198, thereby perturbing the geometry of the active site Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.108 mitochondrion
-
 Homo sapiens 5739
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.108 Homo sapiens O43464
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.21.108 HtrA2
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.108 97.3
-
 melting temperature Homo sapiens