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Structure paper

TitleStructures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 68, Page 1488-1500, Year 2012
Publish dateMay 22, 2012 (structure data deposition date)
AuthorsLee, B.G. / Kim, M.K. / Kim, B.W. / Suh, S.W. / Song, H.K.
External linksActa Crystallogr. ,Sect. D / PubMed:23090398
MethodsX-ray diffraction
Resolution1.7 - 2.3 Å
Structure data

PDB-4fb9:
Structure of mutant RIP from barley seeds
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4fba:
Structure of mutant RIP from barley seeds in complex with adenine
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4fbb:
Structure of mutant RIP from barley seeds in complex with adenine (AMP-incubated)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4fbc:
Structure of mutant RIP from barley seeds in complex with AMP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4fbh:
Structure of RIP from barley seeds
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ADE:
ADENINE

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • hordeum vulgare (barley)
KeywordsHYDROLASE / Ribosome Inactivating Protein / rRNA N-glycosylase activity / ribosome

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