2qx5

From Proteopedia

Revision as of 09:50, 23 January 2008

Structure of nucleoporin Nic96

Overview

The nuclear pore complex (NPC) is an elaborate protein machine that, mediates macromolecular transport across the nuclear envelope in all, eukaryotes. The NPC is formed by nucleoporins that assemble in multiple, copies around an 8-fold symmetry axis. Homology modeling suggests that, most architectural nucleoporins are composed of simple beta-propeller and, alpha-helical repeat domains. Here we present the crystal structure of, Nic96, the Nup93 homolog in Saccharomyces cerevisiae, one of the major, components of the NPC. This is the first structure of an alpha-helical, nucleoporin domain. The protein folds into an elongated, mostly, alpha-helical structure. Characteristically, non-canonical architectural, features define the Nic96 structure. Sequence conservation among Nup93, homologs across all eukaryotes strongly suggests that the distinct, topology is evolutionarily well maintained. We propose that the unique, Nic96/Nup93 fold has a conserved function in all eukaryotes.

About this Structure

2QX5 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of nucleoporin nic96 reveals a novel, intricate helical domain architecture., Jeudy S, Schwartz TU, J Biol Chem. 2007 Nov 30;282(48):34904-12. Epub 2007 Sep 25. PMID:17897938

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