1xk5

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xk5 OCA], [http://www.ebi.ac.uk/pdbsum/1xk5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xk5 RCSB]</span>
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[[Category: Luehrmann, R.]]
[[Category: Luehrmann, R.]]
[[Category: Strasser, A.]]
[[Category: Strasser, A.]]
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[[Category: TPG]]
 
[[Category: protein-rna-complex]]
[[Category: protein-rna-complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:13:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:50:42 2008''

Revision as of 21:50, 30 March 2008


PDB ID 1xk5

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the m3G-cap-binding domain of snurportin1 in complex with a m3GpppG-cap dinucleotide


Overview

In higher eukaryotes the biogenesis of spliceosomal UsnRNPs involves a nucleocytoplasmic shuttling cycle. After the m7G-cap-dependent export of the snRNAs U1, U2, U4 and U5 to the cytoplasm, each of these snRNAs associates with seven Sm proteins. Subsequently, the m7G-cap is hypermethylated to the 2,2,7-trimethylguanosine (m3G)-cap. The import adaptor snurportin1 recognises the m3G-cap and facilitates the nuclear import of the UsnRNPs by binding to importin-beta. Here we report the crystal structure of the m3G-cap-binding domain of snurportin1 with bound m3GpppG at 2.4 A resolution, revealing a structural similarity to the mRNA-guanyly-transferase. Snurportin1 binds both the hypermethylated cap and the first nucleotide of the RNA in a stacked conformation. This binding mode differs significantly from that of the m7G-cap-binding proteins Cap-binding protein 20 (CBP20), eukaryotic initiation factor 4E (eIF4E) and viral protein 39 (VP39). The specificity of the m3G-cap recognition by snurportin1 was evaluated by fluorescence spectroscopy, demonstrating the importance of a highly solvent exposed tryptophan for the discrimination of m7G-capped RNAs. The critical role of this tryptophan and as well of a tryptophan continuing the RNA base stack was confirmed by nuclear import assays and cap-binding activity tests using several snurportin1 mutants.

About this Structure

1XK5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1., Strasser A, Dickmanns A, Luhrmann R, Ficner R, EMBO J. 2005 Jul 6;24(13):2235-43. Epub 2005 May 26. PMID:15920472

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