1z3h: Difference between revisions

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[[Image:1z3h.gif|left|200px]]<br /><applet load="1z3h" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1z3h.gif|left|200px]]
caption="1z3h, resolution 3.100&Aring;" />
 
'''The exportin Cse1 in its cargo-free, cytoplasmic state'''<br />
{{Structure
|PDB= 1z3h |SIZE=350|CAPTION= <scene name='initialview01'>1z3h</scene>, resolution 3.100&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
|ACTIVITY=
|GENE= Cse1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
}}
 
'''The exportin Cse1 in its cargo-free, cytoplasmic state'''
 


==Overview==
==Overview==
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==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 <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].  
1Z3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3H OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15866177 15866177]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15866177 15866177]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: nuclear transport]]
[[Category: nuclear transport]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:45 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:46 2008''

Revision as of 16:30, 20 March 2008

File:1z3h.gif


PDB ID 1z3h

Drag the structure with the mouse to rotate
, resolution 3.100Å
Ligands:
Gene: Cse1 (Saccharomyces cerevisiae)
Coordinates: save as pdb, mmCIF, xml



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. 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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