1gy7

N77Y point mutant of S.Cerevisiae NTF2

spinqualitylabelsall models 1gy7, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gy7 is a 4 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 1.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NTF2_YEAST Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. In vitro, the NTF2-Ran-GDP association, in the presence of GTP, triggers dissociation of the karyopherin alpha-beta complex, allowing nuclear translocation of karyopherin alpha and the NLS substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Interactions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 A resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-beta and TAP/p15 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats.,Bayliss R, Leung SW, Baker RP, Quimby BB, Corbett AH, Stewart M EMBO J. 2002 Jun 17;21(12):2843-53. PMID:12065398 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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