Evidence map›Paper›PMID 27035839›Full record

ArticleACS chemical biology2016

Turnover of Bacterial Cell Wall by SltB3, a Multidomain Lytic Transglycosylase of Pseudomonas aeruginosa.

Mijoon Lee, Teresa Domínguez-Gil, Dusan Hesek, Kiran V Mahasenan, Elena Lastochkin, Juan A Hermoso, Shahriar Mobashery

Erratum issuedAbstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Exolytic and endolytic turnover of peptidoglycan by lytic transglycosylase Slt ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Review
  6. Article
  7. Article
  8. Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017
    Review
  9. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Mijoon LeeDepartment of Chemistry and Biochemistry, University of Notre Dame , Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Teresa Domínguez-GilDepartment of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC , Serrano 119, 28006 Madrid, Spain.
Dusan HesekDepartment of Chemistry and Biochemistry, University of Notre Dame , Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Kiran V MahasenanDepartment of Chemistry and Biochemistry, University of Notre Dame , Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Elena LastochkinDepartment of Chemistry and Biochemistry, University of Notre Dame , Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Juan A HermosoDepartment of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC , Serrano 119, 28006 Madrid, Spain.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame , Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
NIGMS NIH HHS R01 GM061629NIH HHS GM61629
6 · The paper itself

Abstract

A family of 11 lytic transglycosylases in Pseudomonas aeruginosa, an opportunistic human pathogen, turn over the polymeric bacterial cell wall in the course of its recycling, repair, and maturation. The functions of these enzymes are not fully understood. We disclose herein that SltB3 of P. aeruginosa is an exolytic lytic transglycosylase. We characterize its reaction and its products by the use of peptidoglycan-based molecules. The enzyme recognizes a minimum of four sugars in its substrate but can process a substrate comprised of a peptidoglycan of 20 sugars. The ultimate product of the reaction is N-acetylglucosamine-1,6-anhydro-N-acetylmuramic acid. The X-ray structure of this enzyme is reported for the first time. The enzyme is comprised of four domains, arranged within an annular conformation. The polymeric linear peptidoglycan substrate threads through the opening of the annulus, as it experiences turnover.

Indexed as

Catalytic DomainCrystallography, X-RayGlycosyltransferasesHydrogen BondingModels, ChemicalPeptidoglycanPseudomonas aeruginosaGlycosyltransferasesPeptidoglycan

Identifiers

PMID27035839
PMCPMC5436585

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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.