View source for 5fm6


==Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(apo)==
<StructureSection load='5fm6' size='340' side='right'caption='[[5fm6]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FM6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.997&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5fm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fm6 OCA], [https://pdbe.org/5fm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fm6 RCSB], [https://www.ebi.ac.uk/pdbsum/5fm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fm6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0RYI5_CHATD G0RYI5_CHATD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Rvb1/Rvb2 complex is an essential component of many cellular pathways. The Rvb1/Rvb2 complex forms a dodecameric assembly where six copies of each subunit form two heterohexameric rings. However, due to conformational variability, the way the two rings pack together is still not fully understood. Here, we present the crystal structure and two cryo-electron microscopy reconstructions of the dodecameric, full-length Rvb1/Rvb2 complex, all showing that the interaction between the two heterohexameric rings is mediated through the Rvb1/Rvb2-specific domain II. Two conformations of the Rvb1/Rvb2 dodecamer are present in solution: a stretched conformation also present in the crystal, and a compact conformation. Novel asymmetric features observed in the reconstruction of the compact conformation provide additional insight into the plasticity of the Rvb1/Rvb2 complex.

The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.,Silva-Martin N, Dauden MI, Glatt S, Hoffmann NA, Kastritis P, Bork P, Beck M, Muller CW PLoS One. 2016 Jan 8;11(1):e0146457. doi: 10.1371/journal.pone.0146457., eCollection 2016. PMID:26745716<ref>PMID:26745716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fm6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Large Structures]]
[[Category: Dauden MI]]
[[Category: Glatt S]]
[[Category: Hoffmann NA]]
[[Category: Mueller CW]]
[[Category: Silva-Martin N]]