Literature summary for 2.4.2.31 extracted from

Sundriyal, A.; Roberts, A.; Shone, C.; Acharya, K.
Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from Clostridium difficile (2009), J. Biol. Chem., 284, 28713-28719.

Crystallization (Commentary)

Crystallization (Comment)	Organism
catalytic subunit CdtA in its native form at pH 4.0, 8.5, and 9.0 and in complex with ADP-ribose donors, NAD+ and NADPH at pH 9.0. The crystal structures of the native protein show pronounced conformational flexibility confined to the active site region of the protein and enhanced disorder at low pH. The suggested catalytically important residues Glu385 and Glu387 seem to play no role or a less important role in ligand binding	Clostridioides difficile

Crystallization (Comment)

Organism

catalytic subunit CdtA in its native form at pH 4.0, 8.5, and 9.0 and in complex with ADP-ribose donors, NAD+ and NADPH at pH 9.0. The crystal structures of the native protein show pronounced conformational flexibility confined to the active site region of the protein and enhanced disorder at low pH. The suggested catalytically important residues Glu385 and Glu387 seem to play no role or a less important role in ligand binding

Clostridioides difficile

Organism

Organism	UniProt	Comment	Textmining
Clostridioides difficile	Q9KH42	-	-

Synonyms

Synonyms	Comment	Organism
ADP-ribosyltransferase enzymatic component	-	Clostridioides difficile
CdtA	-	Clostridioides difficile

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Release 2023.1 (January 2023)