1xip: Difference between revisions

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[[Image:1xip.jpg|left|200px]]
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[[Image:1xip.png|left|200px]]


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{{STRUCTURE_1xip|  PDB=1xip  |  SCENE=  }}  
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'''Crystal Structure of the N-terminal Domain of Nup159'''
===Crystal Structure of the N-terminal Domain of Nup159===




==Overview==
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Nuclear export of mRNA in eukaryotic cells is mediated by soluble transport factors and components of the nuclear pore complex (NPC). The cytoplasmically oriented nuclear pore protein Nup159 plays a critical role in mRNA export through its conserved N-terminal domain (NTD). Here, we report the crystal structure of the Nup159 NTD, refined to 2.5 A. The structure reveals an unusually asymmetric seven-bladed beta-propeller that is structurally conserved throughout eukarya. Using structure-based conservation analysis, we have targeted specific surface residues for mutagenesis. Residue substitutions in a conserved loop of the NTD abolish in vitro binding to Dbp5, a DEAD box helicase required for mRNA export. In vivo, these mutations cause Dbp5 mislocalization and block mRNA export. These findings suggest that the Nup159 NTD functions in mRNA export as a binding platform, tethering shuttling Dbp5 molecules at the nuclear periphery and locally concentrating this mRNA remodeling factor at the cytoplasmic face of the NPC.
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{{ABSTRACT_PUBMED_15574330}}


==About this Structure==
==About this Structure==
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[[Category: Weis, K.]]
[[Category: Weis, K.]]
[[Category: Beta-propeller]]
[[Category: Beta-propeller]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:05:00 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:00:34 2008''

Revision as of 02:00, 29 July 2008

File:1xip.png

Template:STRUCTURE 1xip

Crystal Structure of the N-terminal Domain of Nup159

Template:ABSTRACT PUBMED 15574330

About this Structure

1XIP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore., Weirich CS, Erzberger JP, Berger JM, Weis K, Mol Cell. 2004 Dec 3;16(5):749-60. PMID:15574330

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