Literature summary for 3.2.2.22 extracted from

Carra, J.H.; McHugh, C.A.; Mulligan, S.; Machiesky, L.M.; Soares, A.S.; Millard, C.B.
Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site (2007), BMC Struct. Biol., 7, 72.

Crystallization (Commentary)

Crystallization (Comment)	Organism
the smallest ligand stabilizing an open conformer of the ricin A chain active site pocket is an amide group, bound weakly by only a few hydrogen bonds to the protein. Complexes with small amide-containing molecules also reveal a switch in geometry from a parallel towards a splayed arrangement of an arginine-tryptophan cation-pi interaction that was associated with an increase and redshift in tryptophan fluorescence upon ligand binding. Urea binding has a favorable enthalpy change and unfavorable entropy change. The side-chain position of residue >80 in a complex with adenine suggests a smaller role for aromatic stacking at the ricin active site	Ricinus communis

Crystallization (Comment)

Organism

the smallest ligand stabilizing an open conformer of the ricin A chain active site pocket is an amide group, bound weakly by only a few hydrogen bonds to the protein. Complexes with small amide-containing molecules also reveal a switch in geometry from a parallel towards a splayed arrangement of an arginine-tryptophan cation-pi interaction that was associated with an increase and redshift in tryptophan fluorescence upon ligand binding. Urea binding has a favorable enthalpy change and unfavorable entropy change. The side-chain position of residue >80 in a complex with adenine suggests a smaller role for aromatic stacking at the ricin active site

Ricinus communis

Organism

Organism	UniProt	Comment	Textmining
Ricinus communis	P02879	ricin A chain	-

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Release 2023.1 (January 2023)