Evidence map›Paper›PMID 27899450›Full record

ArticleThe Journal of biological chemistry2017

Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B.

Dustin T King, Gregory A Wasney, Michael Nosella, Anita Fong, Natalie C J Strynadka

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. ACS infectious diseases · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Adhesion and Colonization of theFrontiers in microbiology · 2022
    Article
  13. Article
  14. Article
  15. The bacterial cell division protein fragmentThe Journal of biological chemistry · 2020
    Article
  16. Potential of 2-Chloro-Molecules (Basel, Switzerland) · 2020
    Article
  17. Regulation of peptidoglycan synthesis and remodelling.Nature reviews. Microbiology · 2020
    Review
  18. Article
  19. Article
  20. Tellimagrandin II, A Type of Plant Polyphenol Extracted fromInternational journal of molecular sciences · 2019
    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

5 authors.

Dustin T KingFrom the Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Gregory A WasneyFrom the Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Michael NosellaFrom the Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Anita FongFrom the Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Natalie C J StrynadkaFrom the Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada ncjs@mail.ubc.ca.

Funding

CIHRHoward Hughes Medical Institute
6 · The paper itself

Abstract

In Escherichia coli, the peptidoglycan cell wall is synthesized by bifunctional penicillin-binding proteins such as PBP1b that have both transpeptidase and transglycosylase activities. The PBP1b transpeptidase domain is a major target of β-lactams, and therefore it is important to attain a detailed understanding of its inhibition. The peptidoglycan glycosyltransferase domain of PBP1b is also considered an excellent antibiotic target yet is not exploited by any clinically approved antibacterials. Herein, we adapt a pyrophosphate sensor assay to monitor PBP1b-catalyzed glycosyltransfer and present an improved crystallographic model for inhibition of the PBP1b glycosyltransferase domain by the potent substrate analog moenomycin. We elucidate the structure of a previously disordered region in the glycosyltransferase active site and discuss its implications with regards to peptidoglycan polymerization. Furthermore, we solve the crystal structures of E. coli PBP1b bound to multiple different β-lactams in the transpeptidase active site and complement these data with gel-based competition assays to provide a detailed structural understanding of its inhibition. Taken together, these biochemical and structural data allow us to propose new insights into inhibition of both enzymatic domains in PBP1b.

Indexed as

beta-LactamsCrystallography, X-RayEscherichia coli K12Escherichia coli ProteinsPenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseProtein DomainsSerine-Type D-Ala-D-Ala Carboxypeptidasebeta-LactamsEscherichia coli Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseSerine-Type D-Ala-D-Ala Carboxypeptidaseantibioticsbacteriaglycosyltransferaseinhibitormoenomycinpenicillin-binding protein 1bpeptidoglycantransglycosylationtranspeptidationβ-lactam

Identifiers

PMID27899450
PMCPMC5247669

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.