Evidence map›Paper›PMID 27112599›Full record

ArticleStructure (London, England : 1993)2016

Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy.

Caroline A Ewens, Min Su, Liang Zhao, Nardin Nano, Walid A Houry, Daniel R Southworth

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Cryo-EM structures of the human INO80 chromatin-remodeling complex.Nature structural & molecular biology · 2018
    Article
  10. Pih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p.Structure (London, England : 1993) · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Caroline A EwensDepartment of Biological Chemistry, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Min SuDepartment of Biological Chemistry, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Liang ZhaoDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Nardin NanoDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Walid A HouryDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Daniel R SouthworthDepartment of Biological Chemistry, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: dsouth@umich.edu.
University of Michigan · USUniversity of Toronto · CA

Funding

Defining the conformational cycle of nitric oxide synthasesR01GM110001 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SOUTHWORTH, DANIEL RYLAND · 2015 to 2019
$1.5M
Silicon Mechanics Compute ClusterS10OD020011 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2015 to 2015
$490k
CIHR MOP-93778NIGMS NIH HHS R01 GM110001NIH HHS S10 OD020011
6 · The paper itself

Abstract

Rvb1 and Rvb2 are essential AAA+ proteins that interact together during the assembly and activity of diverse macromolecules including chromatin remodelers INO80 and SWR-C, and ribonucleoprotein complexes including telomerase and snoRNPs. ATP hydrolysis by Rvb1/2 is required for function; however, the mechanism that drives substrate remodeling is unknown. Here we determined the architecture of the yeast Rvb1/2 dodecamer using cryoelectron microscopy and identify that the substrate-binding insertion domain undergoes conformational changes in response to nucleotide state. 2D and 3D classification defines the dodecamer flexibility, revealing distinct arrangements and the hexamer-hexamer interaction interface. Reconstructions of the apo, ATP, and ADP states identify that Rvb1/2 undergoes substantial conformational changes that include a twist in the insertion-domain position and a corresponding rotation of the AAA+ ring. These results reveal how the ATP hydrolysis cycle of the AAA+ domains directs insertion-domain movements that could provide mechanical force during remodeling or helicase activities.

Indexed as

Molecular Dynamics SimulationATPases Associated with Diverse Cellular ActivitiesBinding SitesCarrier ProteinsCryoelectron MicroscopyDNA HelicasesMolecular Docking SimulationNucleotidesProtein BindingATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesNucleotidesRUVBL1 protein, humanRUVBL2 protein, human

Identifiers

PMID27112599
PMCPMC13429012
OpenAlexW2339725660

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.