Literature summary 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.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.2.2.22 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.2.2.22 |
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
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.2.2.22 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.2.22 |
Zea mays |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.2.2.22 |
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
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.2.2.22 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
3.2.2.22 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.2.22 |
MOD |
- |
Zea mays |
3.2.2.22 |
ribosome inactivating protein |
- |
Zea mays |
3.2.2.22 |
RIP |
- |
Zea mays |
3.2.2.22 |
type III RIP |
- |
Zea mays |