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Literature summary for 3.4.22.69 extracted from

  • Kanitz, M.; Blanck, S.; Heine, A.; Gulyaeva, A.A.; Gorbalenya, A.E.; Ziebuhr, J.; Diederich, W.E.
    Structural basis for catalysis and substrate specificity of a 3C-like cysteine protease from a mosquito mesonivirus (2019), Virology, 533, 21-33 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of free enzyme and the enzyme/peptide aldehyde inhibitor(benzoyl-YYNQ-H) complex by hanging-drop method. The 3CLpro structure (refined to 1.94 A) shows that the protein forms dimers. The monomers are comprised of N-terminal domains I and II, which adopt a chymotrypsin-like fold, and a C-terminal alpha-helical domain III. The catalytic Cys-His dyad is assisted by a complex network of interactions involving a water molecule that mediates polar contacts between the catalytic His and a conserved Asp located in the domain II-III junction and is suitably positioned to stabilize the developing positive charge of the catalytic His in the transition state during catalysis Alphamesonivirus 1

Inhibitors

Inhibitors Comment Organism Structure
benzoyl-YYNQ-H
-
Alphamesonivirus 1

Organism

Organism UniProt Comment Textmining
Alphamesonivirus 1 F8RL29 isolate Aedes harrisoni
-

Purification (Commentary)

Purification (Comment) Organism
-
Alphamesonivirus 1

Synonyms

Synonyms Comment Organism
3C-like cysteine protease
-
Alphamesonivirus 1