5tqb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)== | |||
<StructureSection load='5tqb' size='340' side='right' caption='[[5tqb]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tqb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TQB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tqb OCA], [http://pdbe.org/5tqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tqb RCSB], [http://www.ebi.ac.uk/pdbsum/5tqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tqb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eukaryotic ribosome biogenesis requires the nuclear import of approximately 80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery. | |||
Molecular basis for protection of ribosomal protein L4 from cellular degradation.,Huber FM, Hoelz A Nat Commun. 2017 Feb 2;8:14354. doi: 10.1038/ncomms14354. PMID:28148929<ref>PMID:28148929</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5tqb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hoelz, A]] | |||
[[Category: Huber, F M]] | |||
[[Category: Ribosomal protein]] | |||
[[Category: Ribosome assembly chaperone]] | |||
Revision as of 20:45, 10 March 2017
Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)
Structural highlights
Publication Abstract from PubMedEukaryotic ribosome biogenesis requires the nuclear import of approximately 80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery. Molecular basis for protection of ribosomal protein L4 from cellular degradation.,Huber FM, Hoelz A Nat Commun. 2017 Feb 2;8:14354. doi: 10.1038/ncomms14354. PMID:28148929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||