Evidence map›Paper›PMID 17437715›Full record

ArticleStructure (London, England : 1993)2007

ATP ground- and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54.

Baoyu Chen, Michaeleen Doucleff, David E Wemmer, Sacha De Carlo, Hector H Huang, Eva Nogales, Timothy R Hoover, Elena Kondrashkina, Liang Guo, B Tracy Nixon

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Mechanisms of σJournal of molecular biology · 2019
    Review
  6. Article
  7. Article
  8. Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017
    Review
  9. Role of the σJournal of molecular biology · 2016
    Article
  10. EF-G Activation by Phosphate Analogs.Journal of molecular biology · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Breaking symmetry in multimeric ATPase motors.Cell cycle (Georgetown, Tex.) · 2014
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

10 authors.

Baoyu ChenIntegrative Biosciences Graduate Degree Program, Chemical Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Michaeleen Doucleff
David E Wemmer
Sacha De Carlo
Hector H Huang
Eva Nogales
Timothy R Hoover
Elena Kondrashkina
Liang Guo
B Tracy Nixon

Funding

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
NIGMS NIH HHS R01 GM069937
6 · The paper itself

Abstract

Transcription initiation by the sigma54 form of bacterial RNA polymerase requires hydrolysis of ATP by an enhancer binding protein (EBP). We present SAS-based solution structures of the ATPase domain of the EBP NtrC1 from Aquifex aeolicus in different nucleotide states. Structures of apo protein and that bound to AMPPNP or ADP-BeF(x) (ground-state mimics), ADP-AlF(x) (a transition-state mimic), or ADP (product) show substantial changes in the position of the GAFTGA loops that contact polymerase, particularly upon conversion from the apo state to the ADP-BeF(x) state, and from the ADP-AlF(x) state to the ADP state. Binding of the ATP analogs stabilizes the oligomeric form of the ATPase and its binding to sigma54, with ADP-AlF(x) having the largest effect. These data indicate that ATP binding promotes a conformational change that stabilizes complexes between EBPs and sigma54, while subsequent hydrolysis and phosphate release drive the conformational change needed to open the polymerase/promoter complex.

Indexed as

Enhancer Elements, GeneticAdenosine TriphosphatasesAdenosine TriphosphateBacteriaRNA Polymerase Sigma 54Scattering, Small AngleX-Ray DiffractionAdenosine TriphosphatasesAdenosine TriphosphateRNA Polymerase Sigma 54

Identifiers

PMID17437715
PMCPMC2680074

What OpenQuestion holds

Textmetadata
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.