Evidence map›Paper›PMID 33620038›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis.

Justas V Rodarte, Jan Abendroth, Thomas E Edwards, Donald D Lorimer, Bart L Staker, Sunny Zhang, Peter J Myler, Krystle J McLaughlin

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Structures of Legionella pneumophila serogroup 1 peptide deformylase bound to nickel(II) and actinonin.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  2. Structural characterization of dUTPase from Legionella pneumophila.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  3. Article
  4. Structural and functional characterization of FabG4 from Mycolicibacterium smegmatis.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  5. Characterization of a family I inorganic pyrophosphatase from Legionella pneumophila Philadelphia 1.Acta crystallographica. Section F, Structural biology communications · 2023
    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

8 authors at 2 institutions in 1 country.

Justas V RodarteDepartment of Chemistry, Vassar College, 124 Raymond Avenue, Poughkeepsie, New York, USA.
Jan AbendrothSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Thomas E EdwardsSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Donald D LorimerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Bart L StakerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Sunny ZhangSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.ORCID 0000-0002-7497-3206
Peter J MylerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, Washington, USA.
Krystle J McLaughlinDepartment of Chemistry, Vassar College, 124 Raymond Avenue, Poughkeepsie, New York, USA.
Center for Infectious Disease Research · USVassar College · US

Funding

NIAID NIH HHS HHSN272201200025CNIAID NIH HHS HHSN272201700059C
6 · The paper itself

Abstract

Rickettsia felis, a Gram-negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been shown to be adaptable to a wide range of hosts, and many fevers of unknown origin are now being attributed to this infectious agent. Here, the structure of acetoacetyl-CoA reductase from R. felis is reported at a resolution of 2.0 Å. While R. felis acetoacetyl-CoA reductase shares less than 50% sequence identity with its closest homologs, it adopts a fold common to other short-chain dehydrogenase/reductase (SDR) family members, such as the fatty-acid synthesis II enzyme FabG from the prominent pathogens Staphylococcus aureus and Bacillus anthracis. Continued characterization of the Rickettsia proteome may prove to be an effective means of finding new avenues of treatment through comparative structural studies.

Indexed as

Alcohol OxidoreductasesBacterial ProteinsCrystallography, X-RayModels, MolecularProtein ConformationRickettsia felisacetoacetyl-CoA reductaseAlcohol OxidoreductasesBacterial Proteinsacetoacetyl-CoA reductaseoxidoreductasePhaBRickettsiaSeattle Structural Genomics Center for Infectious DiseaseSSGCIDstructural genomics

Identifiers

PMID33620038
PMCPMC7900926
OpenAlexW2979284552

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.