1XIP

Crystal Structure of the N-terminal Domain of Nup159

Summary for 1XIP

• Entry DOI: 10.2210/pdb1xip/pdb
• Descriptor: Nucleoporin NUP159 (2 entities in total)
• Functional Keywords: beta-propeller, transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus, nuclear pore complex: P40477
• Total number of polymer chains: 1
• Total formula weight: 43177.85

Authors

Weirich, C.S.,Erzberger, J.P.,Berger, J.M.,Weis, K. (deposition date: 2004-09-21, release date: 2004-12-14, Last modification date: 2011-07-13)

Primary citation

Weirich, C.S.,Erzberger, J.P.,Berger, J.M.,Weis, K.
The N-Terminal Domain of Nup159 Forms a beta-Propeller that Functions in mRNA Export by Tethering the Helicase Dbp5 to the Nuclear Pore
Mol.Cell, 16:749-760, 2004

PubMed Abstract: 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.

PubMed: 15574330
DOI: 10.1016/j.molcel.2004.10.032

Experimental method

X-RAY DIFFRACTION (2.5 Å)