Evidence map›Paper›PMID 16618922›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Domain architecture and structure of the bacterial cell division protein DivIB.

Scott A Robson, Glenn F King

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Roles of pneumococcal DivIB in cell division.Journal of bacteriology · 2008
    Article
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Scott A RobsonDepartment of Molecular, Microbial, and Structural Biology and Partnership for Excellence in Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA.
Glenn F King
UConn Health · US

Funding

TOPOLOGICAL REGULATION OF PROKARYOTIC CELL DIVISIONR01AI048583 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KING, GLENN F · 2001 to 2005
$1.5M
NIAID NIH HHS AI048583NIAID NIH HHS R01 AI048583
6 · The paper itself

Abstract

Bacterial cytokinesis requires the coordinated assembly of a complex of proteins, collectively known as the divisome, at the incipient division site. DivIB/FtsQ is a conserved component of the divisome in bacteria with cell walls, suggesting that it plays a role in synthesis and/or remodeling of septal peptidoglycan. We demonstrate that the extracytoplasmic region of DivIB comprises three discrete domains that we designate alpha, beta, and gamma from the N to C terminus. The alpha-domain is proximal to the cytoplasmic membrane and coincident with the polypeptide transport-associated domain that was proposed previously to function as a molecular chaperone. The beta-domain has a unique 3D fold, with no eukaryotic counterpart, and we show that it interconverts between two discrete conformations via cis-trans isomerization of a Tyr-Pro peptide bond. We propose that this isomerization might modulate protein-protein interactions of the flanking alpha- and gamma-domains. The C-terminal gamma-domain is unstructured in the absence of other divisomal proteins, but we show that it is critical for DivIB function.

Indexed as

Amino Acid SequenceBacillaceaeBacillus subtilisBacterial ProteinsCell DivisionEscherichia coli ProteinsMembrane ProteinsModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein FoldingProtein Structure, TertiaryRecombinant ProteinsSequence Homology, Amino AcidBacterial ProteinsDivIB protein, Bacillus subtilisEscherichia coli ProteinsFtsQ protein, E coliMembrane ProteinsRecombinant Proteins

Identifiers

PMID16618922
PMCPMC1458944
OpenAlexW1963680183

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.