2qx5
From Proteopedia
(New page: 200px<br /><applet load="2qx5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qx5, resolution 2.5Å" /> '''Structure of nucleopo...) |
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==Overview== | ==Overview== | ||
| - | The nuclear pore complex (NPC) is an elaborate protein machine that | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal structure of nucleoporin | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17897938 17897938] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jeudy, S.]] | [[Category: Jeudy, S.]] | ||
| - | [[Category: Schwartz, T | + | [[Category: Schwartz, T U.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: mrna transport]] | [[Category: mrna transport]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:04 2008'' |
Revision as of 16:43, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 18:43:04 2008
