1z3h: Difference between revisions
New page: left|200px<br /><applet load="1z3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z3h, resolution 3.100Å" /> '''The exportin Cse1 i... |
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[[Image:1z3h.gif|left|200px]]<br /><applet load="1z3h" size=" | [[Image:1z3h.gif|left|200px]]<br /><applet load="1z3h" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1z3h, resolution 3.100Å" /> | caption="1z3h, resolution 3.100Å" /> | ||
'''The exportin Cse1 in its cargo-free, cytoplasmic state'''<br /> | '''The exportin Cse1 in its cargo-free, cytoplasmic state'''<br /> | ||
==Overview== | ==Overview== | ||
Cse1 mediates nuclear export of importin alpha, the nuclear localization | Cse1 mediates nuclear export of importin alpha, the nuclear localization signal (NLS) import adaptor. We report the 3.1 A resolution structure of cargo-free Cse1, representing this HEAT repeat protein in its cytosolic state. Cse1 is compact, consisting of N- and C-terminal arches that interact to form a ring. Comparison with the structure of cargo-bound Cse1 shows a major conformational change leading to opening of the structure upon cargo binding. The largest structural changes occur within a hinge region centered at HEAT repeat 8. This repeat contains a conserved insertion that connects the RanGTP and importin alpha contact sites and that is essential for binding. In the cargo-free state, the RanGTP binding sites are occluded and the importin alpha sites are distorted. Mutations that destabilize the N- to C-terminal interaction uncouple importin alpha and Ran binding, suggesting that the closed conformation prevents association with importin alpha. | ||
==About this Structure== | ==About this Structure== | ||
1Z3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1Z3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3H OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nuclear transport]] | [[Category: nuclear transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:45 2008'' | ||
Revision as of 17:11, 21 February 2008
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The exportin Cse1 in its cargo-free, cytoplasmic state
OverviewOverview
Cse1 mediates nuclear export of importin alpha, the nuclear localization signal (NLS) import adaptor. We report the 3.1 A resolution structure of cargo-free Cse1, representing this HEAT repeat protein in its cytosolic state. Cse1 is compact, consisting of N- and C-terminal arches that interact to form a ring. Comparison with the structure of cargo-bound Cse1 shows a major conformational change leading to opening of the structure upon cargo binding. The largest structural changes occur within a hinge region centered at HEAT repeat 8. This repeat contains a conserved insertion that connects the RanGTP and importin alpha contact sites and that is essential for binding. In the cargo-free state, the RanGTP binding sites are occluded and the importin alpha sites are distorted. Mutations that destabilize the N- to C-terminal interaction uncouple importin alpha and Ran binding, suggesting that the closed conformation prevents association with importin alpha.
About this StructureAbout this Structure
1Z3H is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding., Cook A, Fernandez E, Lindner D, Ebert J, Schlenstedt G, Conti E, Mol Cell. 2005 Apr 29;18(3):355-67. PMID:15866177
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