1z3h
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1z3h' size='340' side='right'caption='[[1z3h]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='1z3h' size='340' side='right'caption='[[1z3h]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1z3h]] is a 2 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr id=' | + | <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> |
| - | + | <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> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 21: | Line 20: | ||
</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:15866177</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1z3h" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Conti | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Cook | + | [[Category: Conti E]] |
| - | [[Category: Ebert | + | [[Category: Cook A]] |
| - | [[Category: Fernandez | + | [[Category: Ebert J]] |
| - | [[Category: Lindner | + | [[Category: Fernandez E]] |
| - | [[Category: Schlenstedt | + | [[Category: Lindner D]] |
| - | + | [[Category: Schlenstedt G]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
The exportin Cse1 in its cargo-free, cytoplasmic state
| |||||||||||
