Literature summary for 2.4.1.B62 extracted from

Shen, A.; Lupardus, P.J.; Gersch, M.M.; Puri, A.W.; Albrow, V.E.; Garcia, K.C.; Bogyo, M.
Defining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxins (2011), Nat. Struct. Mol. Biol., 18, 364-371.

Search for more literature for 2.4.1.B62

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme contains an internal cysteine protease domain allosterically regulated by the eukaryotic-specific molecule inositol hexakisphosphate. Apo-cysteine protease is in dynamic equilibrium between active and inactive states. Inositol hexakisphosphate dramatically shifts this equilibrium towards an active conformer that is further restrained upon binding a suicide substrate. Residues within a beta-hairpin region functionally couple the inositol hexakisphosphate binding site to the active site	Clostridioides difficile

Crystallization (Comment)

Organism

enzyme contains an internal cysteine protease domain allosterically regulated by the eukaryotic-specific molecule inositol hexakisphosphate. Apo-cysteine protease is in dynamic equilibrium between active and inactive states. Inositol hexakisphosphate dramatically shifts this equilibrium towards an active conformer that is further restrained upon binding a suicide substrate. Residues within a beta-hairpin region functionally couple the inositol hexakisphosphate binding site to the active site

Clostridioides difficile

Organism

Organism	UniProt	Comment	Textmining
Clostridioides difficile	Q189K3	toxin B	-
Clostridioides difficile 630	Q189K3	toxin B	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)