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'''Unreleased structure'''


The entry 6hyd is ON HOLD
==Rea1 Wild type ADP state (tail part)==
<SX load='6hyd' size='340' side='right' viewer='molstar' caption='[[6hyd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hyd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HYD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</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=6hyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hyd OCA], [https://pdbe.org/6hyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hyd RCSB], [https://www.ebi.ac.uk/pdbsum/6hyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hyd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors. The ~5000 amino-acid AAA+ ATPase Rea1 (or Midasin) generates force to mechanically remove assembly factors from pre-60S particles, which promotes their export to the cytosol. Here we present three Rea1 cryoEM structures. We visualise the Rea1 engine, a hexameric ring of AAA+ domains, and identify an alpha-helical bundle of AAA2 as a major ATPase activity regulator. The alpha-helical bundle interferes with nucleotide-induced conformational changes that create a docking site for the substrate binding MIDAS domain on the AAA +ring. Furthermore, we reveal the architecture of the Rea1 linker, which is involved in force generation and extends from the AAA+ ring. The data presented here provide insights into the mechanism of one of the most complex ribosome maturation factors.


Authors: Sosnowski, P., Urnavicius, L., Boland, A., Fagiewicz, R., Busselez, J., Papai, G., Schmidt, H.
The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1.,Sosnowski P, Urnavicius L, Boland A, Fagiewicz R, Busselez J, Papai G, Schmidt H Elife. 2018 Nov 26;7. pii: 39163. doi: 10.7554/eLife.39163. PMID:30460895<ref>PMID:30460895</ref>


Description: Rea1 Wild type ADP state (tail part)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Fagiewicz, R]]
<div class="pdbe-citations 6hyd" style="background-color:#fffaf0;"></div>
[[Category: Boland, A]]
== References ==
[[Category: Busselez, J]]
<references/>
[[Category: Urnavicius, L]]
__TOC__
[[Category: Schmidt, H]]
</SX>
[[Category: Papai, G]]
[[Category: Large Structures]]
[[Category: Sosnowski, P]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Boland A]]
[[Category: Busselez J]]
[[Category: Fagiewicz R]]
[[Category: Papai G]]
[[Category: Schmidt H]]
[[Category: Sosnowski P]]
[[Category: Urnavicius L]]
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