Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
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SYSTEMATIC NAME
IUBMB Comments
rRNA N-glycohydrolase
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
substrate are intact rabbit ribosomes, best substrate, or ribosomes from Aspergillus flavus, low activity, or Zea mays, the latter are poor substrates, depurination of specific sites in rRNA, formation of RNA fragments
ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA
ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA
maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein
maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein
MOD structure determination and comparison using the crystal structure of DELTAN5-MOD, PDB ID 2PQI, and by determination of the NMR solution structure of MOD, PDB ID 2k6H, detailed overview. MOD has shorter beta6 and alphaB segments, probably for accommodating easier substrate binding, and an alpha-helix instead of an antiparallel beta-sheet in the C-terminal domain, which is involved in binding ribosomal protein P2 in some RIPs, compared to type I and II RIPs. The P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region
isozyme RIP1 is synthesized as inactive precursor protein B-32 or proRIP, which is activated by proteolytic cleavage into two polypeptide chains forming the dimeric enzyme, the enzyme can be activated by papain
isozyme RIP1 is synthesized as inactive precursor protein B-32 or proRIP, which is activated by proteolytic cleavage into two polypeptide chains forming the dimeric enzyme, the enzyme can be activated by papain
isozyme RIP2 is synthesized as inactive precursor protein proRIP2, which is activated by proteolytic cleavage into two polypeptide chains forming the dimeric enzyme, the enzyme can be activated by papain
maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs, because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
construction of an active deletion mutant MOD1 of recombinant proRIP1 with reduced activity compared to recombinant RIP1 after activation of both by papain
construction of an active deletion mutant MOD1 of recombinant proRIP1 with reduced activity compared to recombinant RIP1 after activation of both by papain
gene RIP3:2, genomic DNA library screening, DNA and amino acid sequence determination and analyis, RNA mapping and expression profiling, expression is not under control of the Opaque-2 promoter, expression of gene RIP3:2 encoding isozyme RIP2 in Escherichia coli strain BL21(DE3) as N-terminally His-tagged protein
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site
Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities