Evidence map›Paper›PMID 29497015›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

YopT domain of the PfhB2 toxin from Pasteurella multocida: protein expression, characterization, crystallization and crystallographic analysis.

Sanjeev Kumar, Victoria Hedrick, Seema Mattoo

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

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 98% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. Study on the Pathogenic Mechanism ofPathogens (Basel, Switzerland) · 2026
    Review
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

3 authors at 2 institutions in 1 country.

Sanjeev KumarDepartment of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA.
Victoria HedrickBindley Biosciences Center, Purdue University, 1203 West State Street, West Lafayette, IN 47907, USA.
Seema MattooDepartment of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA.
State Street (United States) · USPurdue University West Lafayette · US

Funding

Role of Fic Proteins in Cellular SignalingR01GM100092 · NIGMS · PURDUE UNIVERSITY · PI MATTOO, SEEMA · 2015 to 2019
$1.7M
Indiana Clinical and Translational Sciences Institute CTSI-106564National Institute for General Medical Sciences (NIGMS) R01GM10092NIGMS NIH HHS R01 GM100092Purdue University PI4D-209263U.S. Department of Energy, Office of Science DE-AC02-11357
6 · The paper itself

Abstract

Pasteurella multocida causes respiratory-tract infections in a broad range of animals, as well as opportunistic infections in humans. P. multocida secretes a multidomain toxin called PfhB2, which contains a YopT-like cysteine protease domain at its C-terminus. The YopT domain of PfhB2 contains a well conserved Cys-His-Asp catalytic triad that defines YopT family members, and shares high sequence similarity with the prototype YopT from Yersinia sp. To date, only one crystal structure of a YopT family member has been reported; however, additional structural information is needed to help characterize the varied substrate specificity and enzymatic action of this large protease family. Here, a catalytically inactive C3733S mutant of PfhB2 YopT that provides enhanced protein stability was used with the aim of gaining structural insight into the diversity within the YopT protein family. To this end, the C3733S mutant of PfhB2 YopT has been successfully cloned, overexpressed, purified and crystallized. Diffraction data sets were collected from native crystals to 3.5 Å resolution and a single-wavelength anomalous data set was collected from an iodide-derivative crystal to 3.2 Å resolution. Data pertaining to crystals belonging to space group P3

Indexed as

Bacterial ProteinsBacterial ToxinsBinding SitesCatalytic DomainCrystallizationCrystallography, X-RayCysteine EndopeptidasesModels, MolecularPasteurella multocidaProtein ConformationProtein DomainsBacterial ProteinsBacterial ToxinsCysteine EndopeptidasesPasteurella multocida toxinAvrPphBcatalytic triadcysteine proteasePasteurella multocidaPfhB2 YopT

Identifiers

PMID29497015
PMCPMC5947697
OpenAlexW2791488296

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.