5fm7: Difference between revisions
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==Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)== | ==Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)== | ||
<StructureSection load='5fm7' size='340' side='right' caption='[[5fm7]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5fm7' size='340' side='right'caption='[[5fm7]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fm7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FM7 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5fm7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FM7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FM7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5flv|5flv]], [[5fm6|5fm6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5flv|5flv]], [[5fm6|5fm6]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fm7 OCA], [http://pdbe.org/5fm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5fm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fm7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cbs 144 50]] | [[Category: Cbs 144 50]] | ||
[[Category: Large Structures]] | |||
[[Category: Dauden, M I]] | [[Category: Dauden, M I]] | ||
[[Category: Glatt, S]] | [[Category: Glatt, S]] | ||
Revision as of 10:25, 6 May 2020
Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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