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Literature summary for 3.4.24.89 extracted from

  • Schacherl, M.; Pichlo, C.; Neundorf, I.; Baumann, U.
    Structural basis of proline-proline peptide bond specificity of the metalloprotease Zmp1 implicated in motility of Clostridium difficile (2015), Structure, 23, 1632-1642.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of Zmp1 in its unbound and peptide-bound forms. The structure analysis reveals a fold similar to Bacillus anthracis lethal factor. The structure consists of an upper N-terminal domain and a lower helical C-terminal domain with respect to the active-site helix aalpha4, which harbors two of the three zinc-binding residues His142 and His146 and the catalytic base Glu143 in the typical metalloprotease motif (H142E143TAH146) Clostridioides difficile

Protein Variants

Protein Variants Comment Organism
E143A 18% of wild-type activity Clostridioides difficile
E143A/Y178F complete loss of activity Clostridioides difficile
Y178F 41% of wild-type activity Clostridioides difficile

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Clostridioides difficile
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q183R7
-
-
Clostridioides difficile 630 Q183R7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-EVNPPVPD + H2O
-
Clostridioides difficile acetyl-EVNP + PVPD
-
?
acetyl-EVNPPVPD + H2O
-
Clostridioides difficile 630 acetyl-EVNP + PVPD
-
?
fibrinogen beta-chain + H2O almost complete digestion within 1 h Clostridioides difficile ?
-
?
fibrinogen beta-chain + H2O almost complete digestion within 1 h Clostridioides difficile 630 ?
-
?
Fibronectin + H2O
-
Clostridioides difficile ? poor substrate ?
Fibronectin + H2O
-
Clostridioides difficile 630 ? poor substrate ?

Synonyms

Synonyms Comment Organism
Zmp1
-
Clostridioides difficile