6q83 | pdb_00006q83

Crystal structure of the biportin Pdr6 in complex with UBC9

spinqualitylabelsall models 6q83, resolution 4.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q83 is a 2 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: KAP122, PDR6, YGL016W (Baker's yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KA122_YEAST] Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of the complex composed the large subunit (TOA1) and the small subunit (TOA2) of the general transcription factor IIA (TFIIA). Required for the nuclear import of the RNR2-RNR4 heterodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR). May play a role in regulation of pleiotropic drug resistance. [UBC9_YEAST] E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Publication Abstract from PubMed Importins ferry proteins into nuclei while exportins carry cargoes to the cytoplasm. In the accompanying paper in this issue (Vera Rodriguez et al. 2019. J. Cell Biol. https://doi.org/10.1083/jcb.201812091), we discovered that Pdr6 is a biportin that imports, e.g., the SUMO E2 ligase Ubc9 while depleting the translation factor eIF5A from the nuclear compartment. In this paper, we report the structures of key transport intermediates, namely, of the Ubc9*Pdr6 import complex, of the RanGTP*Pdr6 heterodimer, and of the trimeric RanGTP*Pdr6*eIF5A export complex. These revealed nonlinear transport signals, chaperone-like interactions, and how the RanGTPase system drives Pdr6 to transport Ubc9 and eIF5A in opposite directions. The structures also provide unexpected insights into the evolution of transport selectivity. Specifically, they show that recognition of Ubc9 by Pdr6 differs fundamentally from that of the human Ubc9-importer Importin 13. Likewise, Pdr6 recognizes eIF5A in a nonhomologous manner compared with the mammalian eIF5A-exporter Exportin 4. This suggests that the import of Ubc9 and active nuclear exclusion of eIF5A evolved in different eukaryotic lineages more than once and independently from each other. Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122.,Aksu M, Trakhanov S, Vera Rodriguez A, Gorlich D J Cell Biol. 2019 Apr 25. pii: jcb.201812093. doi: 10.1083/jcb.201812093. PMID:31023722 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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