5fm7: Difference between revisions

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'''Unreleased structure'''
==Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)==
<StructureSection load='5fm7' size='340' side='right' caption='[[5fm7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fm7]] is a 2 chain structure. 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://oca.weizmann.ac.il/oca-docs/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>
<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://oca.weizmann.ac.il/oca-docs/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]</span></td></tr>
</table>
<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 entry 5fm7 is ON HOLD  until Paper Publication
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>


Authors: Silva-Martin, N., Dauden, M.I., Glatt, S., Hoffmann, N.A., Mueller, C.W.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)
<div class="pdbe-citations 5fm7" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Mueller, C.W]]
<references/>
[[Category: Hoffmann, N.A]]
__TOC__
[[Category: Dauden, M.I]]
</StructureSection>
[[Category: Dauden, M I]]
[[Category: Glatt, S]]
[[Category: Glatt, S]]
[[Category: Hoffmann, N A]]
[[Category: Mueller, C W]]
[[Category: Silva-Martin, N]]
[[Category: Silva-Martin, N]]
[[Category: Atp binding protein]]

Revision as of 19:53, 20 January 2016

Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)

Structural highlights

5fm7 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

5fm7, resolution 2.90Å

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OCA
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