3p27 | pdb_00003p27

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

spinqualitylabelsall models 3p27, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3p27 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 2.95Å Ligands: GDP, MSE 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. Publication Abstract from PubMed Eukaryotic cells have several quality control pathways that rely on translation to detect and degrade defective RNAs. Dom34 and Hbs1 are two proteins that are related to translation termination factors and are involved in no-go decay (NGD) and nonfunctional 18S ribosomal RNA (rRNA) decay (18S NRD) pathways that eliminate RNAs that cause strong ribosomal stalls. Here we present the structure of Hbs1 with and without GDP and a low-resolution model of the Dom34-Hbs1 complex. This complex mimics complexes of the elongation factor and transfer RNA or of the translation termination factors eRF1 and eRF3, supporting the idea that it binds to the ribosomal A-site. We show that nucleotide binding by Hbs1 is essential for NGD and 18S NRD. Mutations in Hbs1 that disrupted the interaction between Dom34 and Hbs1 strongly impaired NGD but had almost no effect on 18S NRD. Hence, NGD and 18S NRD could be genetically uncoupled, suggesting that mRNA and rRNA in a stalled translation complex may not always be degraded simultaneously. Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.,van den Elzen AM, Henri J, Lazar N, Gas ME, Durand D, Lacroute F, Nicaise M, van Tilbeurgh H, Seraphin B, Graille M Nat Struct Mol Biol. 2010 Dec;17(12):1446-52. Epub 2010 Nov 21. PMID:21102444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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