Evidence map›Paper›PMID 21070941›Full record

ArticleStructure (London, England : 1993)2010

Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase.

Baoyu Chen, Tatyana A Sysoeva, Saikat Chowdhury, Liang Guo, Sacha De Carlo, Jeffrey A Hanson, Haw Yang, B Tracy Nixon

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Real-time capture of σNature communications · 2025
    Article
  3. Article
  4. Article
  5. SPARC: Structural properties associated with residue constraints.Computational and structural biotechnology journal · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017
    Review
  13. Article
  14. Role of the σJournal of molecular biology · 2016
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Baoyu ChenDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Tatyana A Sysoeva
Saikat Chowdhury
Liang Guo
Sacha De Carlo
Jeffrey A Hanson
Haw Yang
B Tracy Nixon
Pennsylvania State University · USPrinceton University · USArgonne National Laboratory · USCity University of New York · US

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2001 to 2011
$14.4M
Elucidating the Conformational Dynamics of the AAA+ ATPases NtrC1 and NtrCR01GM069937 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI NIXON, B TRACY · 2006 to 2009
$1.3M
Macromolecular X-Ray Crystallography InstrumentS10RR023439 · NCRR · PENNSYLVANIA STATE UNIVERSITY, THE · PI YENNAWAR, NEELA H. · 2007 to 2007
$500k
NCRR NIH HHS 1S10RR023439-01NCRR NIH HHS P41 RR008630NCRR NIH HHS RR-08630NCRR NIH HHS S10 RR023439NIGMS NIH HHS R01 GM069937NIGMS NIH HHS R01 GM069937-01A3
6 · The paper itself

Abstract

The NtrC-like AAA+ ATPases control virulence and other important bacterial activities through delivering mechanical work to σ54-RNA polymerase to activate transcription from σ54-dependent genes. We report the first crystal structure for such an ATPase, NtrC1 of Aquifex aeolicus, in which the catalytic arginine engages the γ-phosphate of ATP. Comparing the new structure with those previously known for apo and ADP-bound states supports a rigid-body displacement model that is consistent with large-scale conformational changes observed by low-resolution methods. First, the arginine finger induces rigid-body roll, extending surface loops above the plane of the ATPase ring to bind σ54. Second, ATP hydrolysis permits Pi release and retraction of the arginine with a reversed roll, remodeling σ54-RNAP. This model provides a fresh perspective on how ATPase subunits interact within the ring-ensemble to promote transcription, directing attention to structural changes on the arginine-finger side of an ATP-bound interface.

Indexed as

Models, MolecularMolecular Dynamics SimulationAdenosine TriphosphatasesAdenosine TriphosphateArginineBacteriaDNA-Directed RNA PolymerasesHydrolysisProtein ConformationTranscription FactorsAdenosine TriphosphatasesAdenosine TriphosphateArginineDNA-Directed RNA PolymerasesTranscription Factors

Identifiers

PMID21070941
PMCPMC3001195
OpenAlexW2160844977

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.