Evidence map›Paper›PMID 28825148›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017

Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida.

Xiongying Tu, John A Latham, Valerie J Klema, Robert L Evans, Chao Li, Judith P Klinman, Carrie M Wilmot

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

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Occurrence, function, and biosynthesis of mycofactocin.Applied microbiology and biotechnology · 2019
    Review
  6. 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

7 authors at 3 institutions in 1 country.

Xiongying TuDepartment of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
John A LathamDepartments of Chemistry, and Molecular and Cellular Biology, University of California, Berkeley, CA, 94720, USA.
Valerie J KlemaDepartment of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
Robert L EvansDepartment of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
Chao LiDepartment of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA.
Judith P KlinmanDepartments of Chemistry, and Molecular and Cellular Biology, University of California, Berkeley, CA, 94720, USA.
Carrie M WilmotDepartment of Biochemistry, Molecular Biology, and Biophysics, and The Biotechnology Institute, University of Minnesota, St Paul, MN, 55108, USA. wilmo004@umn.edu.
Biotechnology Institute · USUniversity of California, Berkeley · USUniversity of Minnesota · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
Catalysis and biogenesis in methylamine dehydrogenaseR01GM066569 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WILMOT, CAROLINE MARY · 2002 to 2015
$4.0M
National Cancer Institute ACB12002National Institute of General Medical Sciences AGM12006National Institute of General Medical Sciences GM118117National Institute of General Medical Sciences GM66569NIGMS NIH HHS R01 GM066569NIGMS NIH HHS R35 GM118117
6 · The paper itself

Abstract

PqqB is an enzyme involved in the biosynthesis of pyrroloquinoline quinone and a distal member of the metallo-β-lactamase (MBL) superfamily. PqqB lacks two residues in the conserved signature motif HxHxDH that makes up the key metal-chelating elements that can bind up to two metal ions at the active site of MBLs and other members of its superfamily. Here, we report crystal structures of PqqB bound to Mn

Indexed as

Bacterial Proteinsbeta-LactamasesBinding SitesCatalytic DomainCrystallography, X-RayHumansMetalsModels, MolecularPQQ CofactorProtein BindingProtein ConformationPseudomonas InfectionsPseudomonas putidaBacterial Proteinsbeta-LactamasesMetalsPqqB protein, Pseudomonas putidaPQQ CofactorMetal-binding plasticityMetallo-β-lactamasePQQPqqBPyrroloquinoline quinoneX-ray crystallography

Identifiers

PMID28825148
PMCPMC5693720
OpenAlexW2747920298

What OpenQuestion holds

Textmetadata
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.