5tky: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 5tky is ON HOLD
==Crystal structure of the co-translational Hsp70 chaperone Ssb in the ATP-bound, open conformation==
<StructureSection load='5tky' size='340' side='right' caption='[[5tky]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tky]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TKY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tky OCA], [http://pdbe.org/5tky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tky RCSB], [http://www.ebi.ac.uk/pdbsum/5tky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tky ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformation at 2.6 A resolution and identify a positively charged region in the alpha-helical lid domain (SBDalpha), which is present in all members of the Ssb-subfamily of Hsp70s. Mutational analysis demonstrates that this region is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. Taken together, our data reveal how Ssb dynamics on the ribosome allows for the efficient interaction with nascent chains upon RAC-mediated activation of ATP hydrolysis.


Authors: Andrea Gumiero, Genis Valentin Gese, Felix Alexander Weyer, Karine Lapouge, Irmgard Sinning
Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.,Gumiero A, Conz C, Gese GV, Zhang Y, Weyer FA, Lapouge K, Kappes J, von Plehwe U, Schermann G, Fitzke E, Wolfle T, Fischer T, Rospert S, Sinning I Nat Commun. 2016 Nov 24;7:13563. doi: 10.1038/ncomms13563. PMID:27882919<ref>PMID:27882919</ref>


Description: Crystal structure of the co-translational Hsp70 chaperone Ssb in the ATP-bound, open conformation
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Andrea Gumiero, Genis Valentin Gese, Felix Alexander Weyer, Karine Lapouge, Irmgard Sinning]]
<div class="pdbe-citations 5tky" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gese, G V]]
[[Category: Gumiero, A]]
[[Category: Lapouge, K]]
[[Category: Sinning, I]]
[[Category: Weyer, F A]]
[[Category: Chaperone]]
[[Category: Hsp70]]
[[Category: Ribosome]]
[[Category: Translation]]
Retrieved from "https://proteopedia.org/5tky"