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Literature summary for 3.2.2.22 extracted from

  • Yang, Y.; Mak, A.N.; Shaw, P.C.; Sze, K.H.
    Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2 (2010), J. Mol. Biol., 395, 897-907.
    View publication on PubMed
Search for more literature for 3.2.2.22

Activating Compound

Activating Compound Comment Organism Structure
additional information 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 Zea mays

Inhibitors

Inhibitors Comment Organism Structure
additional information 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 Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Zea mays ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA ?
-
 ?

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification 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 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ribosome-inactivating proteins, RIPs, are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA Zea mays ?
-
 ?

Subunits

Subunits Comment Organism
More 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 Zea mays

Synonyms

Synonyms Comment Organism
MOD
-
 Zea mays
ribosome inactivating protein
-
 Zea mays
RIP
-
 Zea mays
type III RIP
-
 Zea mays