Evidence map›Paper›PMID 31584010›Full record

ArticleActa crystallographica. Section F, Structural biology communications2019

Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.

Deanna Dahlke Ojennus, Nicholas J Bratt, Kent L Jones, Douglas H Juers

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

Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Adaptive mechanism ofFood science & nutrition · 2022
    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

4 authors at 2 institutions in 1 country.

Deanna Dahlke OjennusDepartment of Chemistry, Whitworth University, 300 West Hawthorne Road, Spokane, WA 99251, USA.ORCID 0000-0003-4658-2280
Nicholas J BrattDepartment of Chemistry, Whitworth University, 300 West Hawthorne Road, Spokane, WA 99251, USA.ORCID 0000-0002-3063-3939
Kent L JonesDepartment of Mathematics and Computer Science, Whitworth University, 300 West Hawthorne Road, Spokane, WA 99251, USA.ORCID 0000-0003-1773-5559
Douglas H JuersDepartment of Physics and Program in Biochemistry, Biophysics and Molecular Biology, Whitman College, 345 Boyer Avenue, Walla Walla, WA 99632, USA.ORCID 0000-0003-0627-6713
Whitworth University · USWhitman College · US

Funding

National Science Foundation 0723283
6 · The paper itself

Abstract

Prolyl aminodipeptidase (PepX) is an enzyme that hydrolyzes peptide bonds from the N-terminus of substrates when the penultimate amino-acid residue is a proline. Prolyl peptidases are of particular interest owing to their ability to hydrolyze food allergens that contain a high percentage of proline residues. PepX from Lactobacillus helveticus was cloned and expressed in Escherichia coli as an N-terminally His-tagged recombinant construct and was crystallized by hanging-drop vapor diffusion in a phosphate buffer using PEG 3350 as a precipitant. The structure was determined at 2.0 Å resolution by molecular replacement using the structure of PepX from Lactococcus lactis (PDB entry 1lns) as the starting model. Notable differences between the L. helveticus PepX structure and PDB entry 1lns include a cysteine instead of a phenylalanine at the substrate-binding site in the position which confers exopeptidase activity and the presence of a calcium ion coordinated by a calcium-binding motif with the consensus sequence DX(DN)XDG.

Indexed as

AminopeptidasesBacterial ProteinsBinding SitesCalciumCloning, MolecularCrystallography, X-RayCysteineEscherichia coliGlutensLactobacillus helveticusModels, MolecularProtein ConformationRecombinant ProteinsAminopeptidasesBacterial ProteinsCalciumCysteineGlutensprolyl aminopeptidaseRecombinant Proteinscalcium bindingcalcium-blade zoneglutenLactobacillus helveticusPepXprolyl aminodipeptidaseprotein structureα/β-hydrolases

Identifiers

PMID31584010
PMCPMC6777133
OpenAlexW2974204575

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.