Evidence map›Paper›PMID 16030223›Full record

ArticleJournal of bacteriology2005

Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis.

Fiona McArthur, C Evalena Andersson, Slade Loutet, Sherry L Mowbray, Miguel A Valvano

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2005. 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
0.9field-weighted citation impact, top 29% 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, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. ADP-heptose: a bacterial PAMP detected by the host sensor ALPK1.Cellular and molecular life sciences : CMLS · 2021
    Review
  4. Biosynthesis of GDP-d-Biochemistry · 2019
    Article
  5. d-Sedoheptulose-7-phosphate is a common precursor for the heptoses of septacidin and hygromycin B.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. HldE Is Important for Virulence Phenotypes in EnterotoxigenicFrontiers in cellular and infection microbiology · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  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

5 authors at 3 institutions in 2 countries.

Fiona McArthurDepartment of Microbiology and Immunology, Siebens Drake Research Institute, Schulich School of Medicine, University of Western Ontario, London, Ontario N6A 5C1, Canada.
C Evalena Andersson
Slade Loutet
Sherry L Mowbray
Miguel A Valvano
Swedish University of Agricultural Sciences · SEUppsala University · SEWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The core oligosaccharide component of the lipopolysaccharide can be subdivided into inner and outer core regions. In Escherichia coli, the inner core consists of two 3-deoxy-d-manno-octulosonic acid and three glycero-manno-heptose residues. The HldE protein participates in the biosynthesis of ADP-glycero-manno-heptose precursors used in the assembly of the inner core. HldE comprises two functional domains: an N-terminal region with homology to the ribokinase superfamily (HldE1 domain) and a C-terminal region with homology to the cytidylyltransferase superfamily (HldE2 domain). We have employed the structure of the E. coli ribokinase as a template to model the HldE1 domain and predict critical amino acids required for enzyme activity. Mutation of these residues renders the protein inactive as determined in vivo by functional complementation analysis. However, these mutations did not affect the secondary or tertiary structure of purified HldE1, as judged by fluorescence spectroscopy and circular dichroism. Furthermore, in vivo coexpression of wild-type, chromosomally encoded HldE and mutant HldE1 proteins with amino acid substitutions in the predicted ATP binding site caused a dominant negative phenotype as revealed by increased bacterial sensitivity to novobiocin. Copurification experiments demonstrated that HldE and HldE1 form a complex in vivo. Gel filtration chromatography resulted in the detection of a dimer as the predominant form of the native HldE1 protein. Altogether, our data support the notions that the HldE functional unit is a dimer and that structural components present in each HldE1 monomer are required for enzymatic activity.

Indexed as

Adenosine DiphosphateAmino Acid SequenceEscherichia coliHeptosesModels, MolecularMolecular Sequence DataMultienzyme ComplexesNucleotidyltransferasesPhosphotransferases (Alcohol Group Acceptor)Protein Structure, TertiarySequence AlignmentStructure-Activity RelationshipTemplates, GeneticAdenosine DiphosphateD,D heptose 7-phosphate kinase-D,D-heptose 1-phosphate adenylyltransferase, E coliglycero-manno-heptoseHeptosesMultienzyme ComplexesNucleotidyltransferasesPhosphotransferases (Alcohol Group Acceptor)ribokinase

Identifiers

PMID16030223
PMCPMC1196024
OpenAlexW1970369638

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.