Evidence map›Paper›PMID 22467878›Full record

ArticleThe Journal of biological chemistry2012

Regulation of the type IV secretion ATPase TrwD by magnesium: implications for catalytic mechanism of the secretion ATPase superfamily.

Jorge Ripoll-Rozada, Alejandro Peña, Susana Rivas, Fernando Moro, Fernando de la Cruz, Elena Cabezón, Ignacio Arechaga

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Structural organisation of the type IV secretion systems.Current opinion in microbiology · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. 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

7 authors at 3 institutions in 1 country.

Jorge Ripoll-RozadaDepartamento de Biología Molecular, Universidad de Cantabria (UC) e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), 39011 Santander.
Alejandro PeñaDepartamento de Biología Molecular, Universidad de Cantabria (UC) e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), 39011 Santander.
Susana RivasUnidad de Biofísica (CSIC-UPV/EH) y Departamento de Bioquímica y Biología Molecular, Universidad del País Vasco, Apartado 644, 48080 Bilbao, Spain.
Fernando MoroUnidad de Biofísica (CSIC-UPV/EH) y Departamento de Bioquímica y Biología Molecular, Universidad del País Vasco, Apartado 644, 48080 Bilbao, Spain.
Fernando de la CruzDepartamento de Biología Molecular, Universidad de Cantabria (UC) e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), 39011 Santander.
Elena CabezónDepartamento de Biología Molecular, Universidad de Cantabria (UC) e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), 39011 Santander. Electronic address: cabezone@unican.es.
Ignacio ArechagaDepartamento de Biología Molecular, Universidad de Cantabria (UC) e Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), 39011 Santander. Electronic address: arechagai@unican.es.
Instituto de Biomedicina y Biotecnología de Cantabria · ESConsejo Superior de Investigaciones Científicas · ESUniversity of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TrwD, the VirB11 homologue in conjugative plasmid R388, is a member of the large secretion ATPase superfamily, which includes ATPases from bacterial type II and type IV secretion systems, type IV pilus, and archaeal flagellae assembly. Based on structural studies of the VirB11 homologues in Helicobacter pylori and Brucella suis and the archaeal type II secretion ATPase GspE, a unified mechanism for the secretion ATPase superfamily has been proposed. Here, we have found that the ATP turnover of TrwD is down-regulated by physiological concentrations of magnesium. This regulation is exerted by increasing the affinity for ADP, hence delaying product release. Circular dichroism and limited proteolysis analysis indicate that magnesium induces conformational changes in the protein that promote a more rigid, but less active, form of the enzyme. The results shown here provide new insights into the catalytic mechanism of the secretion ATPase superfamily.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsBacterial Secretion SystemsBrucella suisHelicobacter pyloriPlasmidsAdenosine TriphosphatasesBacterial ProteinsBacterial Secretion Systems

Identifiers

PMID22467878
PMCPMC3366828
OpenAlexW1970191255

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.