Evidence map›Paper›PMID 24988330›Full record

ArticleACS chemical biology2014

Structure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coli.

Cecilia Artola-Recolons, Mijoon Lee, Noelia Bernardo-García, Blas Blázquez, Dusan Hesek, Sergio G Bartual, Kiran V Mahasenan, Elena Lastochkin, Hualiang Pi, Bill Boggess and 5 more

Abstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Structural Insights into MltC fromJournal of microbiology and biotechnology · 2026
    Article
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  8. Review
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  10. β-Lactam Resistance inJournal of bacteriology · 2022
    Article
  11. Article
  12. Article
  13. Structural changes in bacteriophage T7 upon receptor-induced genome ejection.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Biofilm Formation byApplied and environmental microbiology · 2021
    Article
  15. Integrative structural biology of the penicillin-binding protein-1 fromComputational and structural biotechnology journal · 2021
    Article
  16. Article
  17. Article
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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

15 authors at 3 institutions in 2 countries.

Cecilia Artola-RecolonsDepartment of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC , Serrano 119, 28006 Madrid, Spain.
Mijoon Lee
Noelia Bernardo-García
Blas Blázquez
Dusan Hesek
Sergio G Bartual
Kiran V Mahasenan
Elena Lastochkin
Hualiang Pi
Bill Boggess
Kathrin Meindl
Isabel Usón
Jed F Fisher
Shahriar Mobashery
Juan A Hermoso
University of Notre Dame · USInstituto de Química Física Blas Cabrera · ESInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
NIGMS NIH HHS GM61629NIGMS NIH HHS R01 GM061629
6 · The paper itself

Abstract

The lytic transglycosylases are essential bacterial enzymes that catalyze the nonhydrolytic cleavage of the glycan strands of the bacterial cell wall. We describe here the structural and catalytic properties of MltC, one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The 2.3 Å resolution X-ray structure of a soluble construct of MltC shows a unique, compared to known lytic transglycosylase structures, two-domain structure characterized by an expansive active site of 53 Å length extending through an interface between the domains. The structures of three complexes of MltC with cell wall analogues suggest the positioning of the peptidoglycan in the active site both as a substrate and as a product. One complex is suggested to correspond to an intermediate in the course of sequential and exolytic cleavage of the peptidoglycan. Moreover, MltC partitioned its reactive oxocarbenium-like intermediate between trapping by the C6-hydroxyl of the muramyl moiety (lytic transglycosylase activity, the major path) and by water (muramidase activity). Genomic analysis identifies the presence of an MltC homologue in no less than 791 bacterial genomes. While the role of MltC in cell wall assembly and maturation remains uncertain, we propose a functional role for this enzyme as befits the uniqueness of its two-domain structure.

Indexed as

Catalytic DomainCell WallCloning, MolecularCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGlycosyltransferasesModels, MolecularMutationPeptidoglycanProtein ConformationProtein Structure, TertiaryEscherichia coli ProteinsGlycosyltransferasesMltC protein, E coliPeptidoglycan

Identifiers

PMID24988330
PMCPMC4168783
OpenAlexW2016794432

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.