Literature summary for 3.2.2.22 extracted from

Mak, A.N.; Wong, Y.T.; An, Y.J.; Cha, S.S.; Sze, K.H.; Au, S.W.; Wong, K.B.; Shaw, P.C.
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site (2007), Nucleic Acids Res., 35, 6259-6267.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of precursor protein and active form, at 2.4 and 2.5 A resolution, respectively. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. Presence of this region diminishes both the interaction with ribosome and cytotoxicity, but not cellular uptake. The active site of the enzyme is too small to accomodate two glutamate residues	Zea mays

Crystallization (Comment)

Organism

crystallization of precursor protein and active form, at 2.4 and 2.5 A resolution, respectively. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. Presence of this region diminishes both the interaction with ribosome and cytotoxicity, but not cellular uptake. The active site of the enzyme is too small to accomodate two glutamate residues

Zea mays

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	class III ribosome-inactivating protein	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	enzyme is synthesized as an inactive precursor with a 25-amino acid internal inactivation region, which is removed in the active form	Zea mays

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Release 2023.1 (January 2023)