1of5 | pdb_00001of5

Crystal structure of Mex67-Mtr2

spinqualitylabelsall models 1of5, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1of5 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 2.8Å Ligands: HG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MEX67_YEAST Involved in the export of mRNA from the nucleus to the cytoplasm. 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 The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP-p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8-A resolution crystal structure of Mtr2 in complex with the NTF2-like domain of Mex67. Mtr2 is a novel member of the NTF2-like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP-p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit. Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.,Fribourg S, Conti E EMBO Rep. 2003 Jul;4(7):699-703. PMID:12835756 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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