Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.
antibiotic resistance
antibiotics
di-metal scaffold
infectious diseases
metallo-β-lactamase
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
08
10
2019
revised:
10
12
2019
accepted:
11
12
2019
pubmed:
18
12
2019
medline:
3
2
2021
entrez:
18
12
2019
Statut:
ppublish
Résumé
Emergence of Enterobacteriaceae harboring metallo-β-lactamases (MBL) has raised global threats due to their broad antibiotic resistance profiles and the lack of effective inhibitors against them. We have been studied one of the emerging environmental MBL, the L1 from Stenotrophomonas maltophilia K279a. We determined several crystal structures of L1 complexes with three different classes of β-lactam antibiotics (penicillin G, moxalactam, meropenem, and imipenem), with the inhibitor captopril and different metal ions (Zn
Identifiants
pubmed: 31846104
doi: 10.1002/pro.3804
pmc: PMC7020990
doi:
Substances chimiques
Anti-Bacterial Agents
0
Lactams
0
Metals, Heavy
0
beta-Lactamase Inhibitors
0
beta-lactamase L1
EC 3.5.2.-
beta-Lactamases
EC 3.5.2.6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
723-743Subventions
Organisme : HHS
ID : HHSN272201700060C
Pays : United States
Organisme : HHS
ID : HHSN272201200026C
Pays : United States
Organisme : NIAID NIH HHS
Pays : United States
Informations de copyright
© 2019 The Authors. Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society.
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