Evidence map›Paper›PMID 28100776›Full record

ArticleThe Journal of biological chemistry2017

Crystallographic Snapshots of Class A β-Lactamase Catalysis Reveal Structural Changes That Facilitate β-Lactam Hydrolysis.

Xuehua Pan, Yunjiao He, Jinping Lei, Xuhui Huang, Yanxiang Zhao

Open access · hybridAbstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.0field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Microbiology spectrum · 2023
    Article
  2. Article
  3. Review
  4. ACS infectious diseases · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Mechanism of proton transfer in class A β-lactamase catalysis and inhibition by avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Crystal Structure of Phosphoserine BlaC fromInternational journal of molecular sciences · 2019
    Article
  14. 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 at 2 institutions in 2 countries.

Xuehua PanFrom the Department of Applied Biology and Chemical Technology, State Key Laboratory of Chirosciences, Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong.
Yunjiao HeFrom the Department of Applied Biology and Chemical Technology, State Key Laboratory of Chirosciences, Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong.
Jinping Leithe Department of Chemistry, Center of Systems Biology and Human Health, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
Xuhui Huangthe Department of Chemistry, Center of Systems Biology and Human Health, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.ORCID 0000-0002-7119-9358
Yanxiang ZhaoFrom the Department of Applied Biology and Chemical Technology, State Key Laboratory of Chirosciences, Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, yanxiang.zhao@polyu.edu.hk.ORCID 0000-0002-9408-9979
Hong Kong Polytechnic University · HKHong Kong University of Science and Technology · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactamases confer resistance to β-lactam-based antibiotics. There is great interest in understanding their mechanisms to enable the development of β-lactamase-specific inhibitors. The mechanism of class A β-lactamases has been studied extensively, revealing Lys-73 and Glu-166 as general bases that assist the catalytic residue Ser-70. However, the specific roles of these two residues within the catalytic cycle remain not fully understood. To help resolve this, we first identified an E166H mutant that is functional but is kinetically slow. We then carried out time-resolved crystallographic study of a full cycle of the catalytic reaction. We obtained structures that represent apo,

Indexed as

AcylationAnti-Bacterial Agentsbeta-Lactamasesbeta-LactamsCatalysisCatalytic DomainCrystallography, X-RayModels, MolecularMutationProtein ConformationAnti-Bacterial Agentsbeta-Lactamasesbeta-Lactamsantibiotic resistanceenzyme catalysisenzyme kineticsstructure-functionX-ray crystallography

Identifiers

PMID28100776
PMCPMC5354505
OpenAlexW2576373510

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.