3p26

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Crystal structure of S. cerevisiae Hbs1 protein (apo-form), a translational GTPase involved in RNA quality control pathways and interacting with Dom34/PelotaCrystal structure of S. cerevisiae Hbs1 protein (apo-form), a translational GTPase involved in RNA quality control pathways and interacting with Dom34/Pelota

Structural highlights

3p26 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBS1_YEAST Involved in protein translation. Together with DOM34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.[1]

References

  1. Doma MK, Parker R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature. 2006 Mar 23;440(7083):561-4. PMID:16554824 doi:nature04530

3p26, resolution 2.50Å

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OCA