1z3h: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1z3h.gif|left|200px]]


{{Structure
==The exportin Cse1 in its cargo-free, cytoplasmic state==
|PDB= 1z3h |SIZE=350|CAPTION= <scene name='initialview01'>1z3h</scene>, resolution 3.100&Aring;
<StructureSection load='1z3h' size='340' side='right'caption='[[1z3h]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
<table><tr><td colspan='2'>[[1z3h]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z3H FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
|GENE= Cse1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3h OCA], [https://pdbe.org/1z3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z3h RCSB], [https://www.ebi.ac.uk/pdbsum/1z3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z3h ProSAT]</span></td></tr>
|RELATEDENTRY=[[1wa5|1wa5]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3h OCA], [http://www.ebi.ac.uk/pdbsum/1z3h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z3h RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CSE1_YEAST CSE1_YEAST] Export receptor for importin alpha (SRP1). Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm.<ref>PMID:9744791</ref> <ref>PMID:9857050</ref> <ref>PMID:9774694</ref> <ref>PMID:10394916</ref>
 
== Evolutionary Conservation ==
'''The exportin Cse1 in its cargo-free, cytoplasmic state'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z3/1z3h_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
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].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z3h ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
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]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Conti E]]
[[Category: Conti, E.]]
[[Category: Cook A]]
[[Category: Cook, A.]]
[[Category: Ebert J]]
[[Category: Ebert, J.]]
[[Category: Fernandez E]]
[[Category: Fernandez, E.]]
[[Category: Lindner D]]
[[Category: Lindner, D.]]
[[Category: Schlenstedt G]]
[[Category: Schlenstedt, G.]]
[[Category: cse1]]
[[Category: exportin]]
[[Category: heat repeat]]
[[Category: nuclear transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:28:30 2008''

Latest revision as of 13:38, 13 March 2024

The exportin Cse1 in its cargo-free, cytoplasmic state

1z3h, resolution 3.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1z3h&oldid=4088253"