Evidence map›Paper›PMID 21246636›Full record

ArticleProteins2011

Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens.

Ritcha Mehra-Chaudhary, Jacob Mick, John J Tanner, Michael T Henzl, Lesa J Beamer

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Mutation of Eamy_RS26425,Applied and environmental microbiology · 2026
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  3. A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026
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  5. Characterization of theAntimicrobial agents and chemotherapy · 2024
    Article
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  7. Article
  8. Mechanistic Studies andJournal of medicinal chemistry · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Advances in protein chemistry and structural biology · 2017
    Article
  17. Article
  18. Review
  19. Article
  20. 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 1 institution in 1 country.

Ritcha Mehra-ChaudharyDepartment of Biochemistry, University of Missouri, Columbia, Missouri 65211, USA.
Jacob Mick
John J Tanner
Michael T Henzl
Lesa J Beamer
University of Missouri · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI RAO, ANJANA · 2001 to 2011
$28.2M
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301
6 · The paper itself

Abstract

The crystal structure of the enzyme phosphoglucomutase from Salmonella typhimurium (StPGM) is reported at 1.7 A resolution. This is the first high-resolution structural characterization of a bacterial protein from this large enzyme family, which has a central role in metabolism and is also important to bacterial virulence and infectivity. A comparison of the active site of StPGM with that of other phosphoglucomutases reveals conserved residues that are likely involved in catalysis and ligand binding for the entire enzyme family. An alternate crystal form of StPGM and normal mode analysis give insights into conformational changes of the C-terminal domain that occur upon ligand binding. A novel observation from the StPGM structure is an apparent dimer in the asymmetric unit of the crystal, mediated largely through contacts in an N-terminal helix. Analytical ultracentrifugation and small-angle X-ray scattering confirm that StPGM forms a dimer in solution. Multiple sequence alignments and phylogenetic studies show that a distinct subset of bacterial PGMs share the signature dimerization helix, while other bacterial and eukaryotic PGMs are likely monomers. These structural, biochemical, and bioinformatic studies of StPGM provide insights into the large α-D-phosphohexomutase enzyme superfamily to which it belongs, and are also relevant to the design of inhibitors specific to the bacterial PGMs.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallography, X-RayMolecular Sequence DataPhosphoglucomutasePhylogenyProtein ConformationProtein MultimerizationProtein SubunitsSalmonella typhimuriumScattering, Small AngleSequence AlignmentVirulenceBacterial ProteinsPhosphoglucomutaseProtein Subunits

Identifiers

PMID21246636
PMCPMC3066478
OpenAlexW2097078121

What OpenQuestion holds

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LicenceTDM
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.