4fb9

X-ray diffraction
1.75Å resolution

Structure of mutant RIP from barley seeds

Released:
Source organism: Hordeum vulgare
Primary publication:
Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism.
Acta Crystallogr D Biol Crystallogr 68 1488-500 (2012)
PMID: 23090398

Function and Biology Details

Reaction catalysed:
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-149558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein synthesis inhibitor I Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 282 amino acids
Theoretical weight: 30.04 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22244 (Residues: 2-281; Coverage: 100%)
Gene name: RIP30
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 130.284Å b: 141.908Å c: 84.819Å
α: 90° β: 126.92° γ: 90°
R-values:
R R work R free
0.171 0.171 0.197
Expression system: Escherichia coli BL21(DE3)