3vwa | pdb_00003vwa

Crystal structure of Cex1p

spinqualitylabelsall models 3vwa, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vwa is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: CEX1, O3240, YOR112W, YOR3240w (Saccharomyces cerevisiae S288c) Resources: FirstGlance, OCA, RCSB, PDBsum Function [CEX1_YEAST] Component of the nuclear tRNA export machinery that my collect tRNA from the nuclear tRNA export receptors of the aminoacylation-dependent export and may deliver aminoacylated tRNAs to the translation machinery pathway at the nuclear pore complex. Publication Abstract from PubMed In all eukaryotes, transcribed precursor tRNAs are maturated by processing and modification processes in nucleus and are transported to the cytoplasm. The cytoplasmic export protein (Cex1p) captures mature tRNAs from the nuclear export receptor (Los1p) on the cytoplasmic side of the nuclear pore complex, and it delivers them to eukaryotic elongation factor 1alpha. This conserved Cex1p function is essential for the quality control of mature tRNAs to ensure accurate translation. However, the structural basis of how Cex1p recognizes tRNAs and shuttles them to the translational apparatus remains unclear. Here, we solved the 2.2 A resolution crystal structure of Saccharomyces cerevisiae Cex1p with C-terminal 197 disordered residues truncated. Cex1p adopts an elongated architecture, consisting of N-terminal kinase-like and a C-terminal alpha-helical HEAT repeat domains. Structure-based biochemical analyses suggested that Cex1p binds tRNAs on its inner side, using the positively charged HEAT repeat surface and the C-terminal disordered region. The N-terminal kinase-like domain acts as a scaffold to interact with the Ran-exportin (Los1p.Gsp1p) machinery. These results provide the structural basis of Los1p.Gsp1p.Cex1p.tRNA complex formation, thus clarifying the dynamic mechanism of tRNA shuttling from exportin to the translational apparatus. Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm.,Nozawa K, Ishitani R, Yoshihisa T, Sato M, Arisaka F, Kanamaru S, Dohmae N, Mangroo D, Senger B, Becker HD, Nureki O Nucleic Acids Res. 2013 Apr 1;41(6):3901-14. doi: 10.1093/nar/gkt010. Epub 2013, Feb 8. PMID:23396276 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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