Home > Publications database > Binding mode of Isoxazolyl Penicillins to a Class-A β-lactamase at ambient conditions > print

001     642342
005     20260112212236.0
024 7 _ |a 10.1038/s42004-025-01801-x
|2 doi
024 7 _ |a 10.3204/PUBDB-2025-05497
|2 datacite_doi
037 _ _ |a PUBDB-2025-05497
041 _ _ |a English
082 _ _ |a 540
100 1 _ |a Gore, Gargi
|0 P:(DE-H253)PIP1099521
|b 0
245 _ _ |a Binding mode of Isoxazolyl Penicillins to a Class-A β-lactamase at ambient conditions
260 _ _ |a [London]
|c 2025
|b Macmillan Publishers Limited, part of Springer Nature
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1768224391_2487194
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a The predominant resistance mechanism observed in Gram-negative bacteria involves the production of β-lactamases, which catalyse the hydrolysis of β-lactam antibiotics, thereby rendering them ineffective. Although Isoxazolyl Penicillins have been available since the 1970s, there are currently no structures in complex with class-A β-lactamases available. Here we have analysed the structure of the clinically relevant β-lactamase CTX-M-14 from Klebsiella pneumoniae near physiological temperatures, via serial synchrotron crystallography. We demonstrate the acyl-enzyme intermediates of the catalytically impaired CTX-M-14 mutant E166A in complex with three Isoxazolyl-Penicillins: Oxacillin, Cloxacillin and Dicloxacillin. Structural comparisons of CTX-M-Penicillin complexes show that, while conserved active-site interactions are maintained, each Isoxazolyl-Penicillin adopts a distinct conformation. While the three derivatives differ only by one and two chlorine atoms, respectively, their conformational heterogeneity appears to be increased by chlorination of the phenyl ring.
536 _ _ |a DFG project G:(GEPRIS)458246365 - Zeitaufgelöste Strukturanalysde der extended spectrum Beta-Lactamase CTX-M-14 (458246365)
|0 G:(GEPRIS)458246365
|c 458246365
|x 0
536 _ _ |a 899 - ohne Topic (POF4-899)
|0 G:(DE-HGF)POF4-899
|c POF4-899
|f POF IV
|x 1
588 _ _ |a Dataset connected to CrossRef, Journals: bib-pubdb1.desy.de
693 _ _ |0 EXP:(DE-MLZ)NOSPEC-20140101
|5 EXP:(DE-MLZ)NOSPEC-20140101
|e No specific instrument
|x 0
700 1 _ |a Prester, Andreas
|b 1
700 1 _ |a von Stetten, David
|0 P:(DE-H253)PIP1083129
|b 2
700 1 _ |a Bartels, Kim
|0 P:(DE-H253)PIP1081587
|b 3
700 1 _ |a Schulz, Eike C.
|0 P:(DE-H253)PIP1019225
|b 4
|e Corresponding author
773 _ _ |a 10.1038/s42004-025-01801-x
|g Vol. 8, no. 1, p. 387
|0 PERI:(DE-600)2929562-2
|n 1
|p 387
|t Communications chemistry
|v 8
|y 2025
|x 2399-3669
856 4 _ |y OpenAccess
|u https://bib-pubdb1.desy.de/record/642342/files/s42004-025-01801-x.pdf
856 4 _ |y OpenAccess
|x pdfa
|u https://bib-pubdb1.desy.de/record/642342/files/s42004-025-01801-x.pdf?subformat=pdfa
909 C O |o oai:bib-pubdb1.desy.de:642342
|p openaire
|p open_access
|p VDB
|p driver
|p dnbdelivery
910 1 _ |a External Institute
|0 I:(DE-HGF)0
|k Extern
|b 0
|6 P:(DE-H253)PIP1099521
910 1 _ |a External Institute
|0 I:(DE-HGF)0
|k Extern
|b 2
|6 P:(DE-H253)PIP1083129
910 1 _ |a European Molecular Biology Laboratory
|0 I:(DE-588b)235011-7
|k EMBL
|b 3
|6 P:(DE-H253)PIP1081587
910 1 _ |a Centre for Structural Systems Biology
|0 I:(DE-H253)_CSSB-20140311
|k CSSB
|b 3
|6 P:(DE-H253)PIP1081587
910 1 _ |a External Institute
|0 I:(DE-HGF)0
|k Extern
|b 4
|6 P:(DE-H253)PIP1019225
913 1 _ |a DE-HGF
|b Programmungebundene Forschung
|l ohne Programm
|1 G:(DE-HGF)POF4-890
|0 G:(DE-HGF)POF4-899
|3 G:(DE-HGF)POF4
|2 G:(DE-HGF)POF4-800
|4 G:(DE-HGF)POF
|v ohne Topic
|x 0
914 1 _ |y 2025
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0160
|2 StatID
|b Essential Science Indicators
|d 2024-12-10
915 _ _ |a Creative Commons Attribution CC BY 4.0
|0 LIC:(DE-HGF)CCBY4
|2 HGFVOC
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0600
|2 StatID
|b Ebsco Academic Search
|d 2024-12-10
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b COMMUN CHEM : 2022
|d 2024-12-10
915 _ _ |a IF >= 5
|0 StatID:(DE-HGF)9905
|2 StatID
|b COMMUN CHEM : 2022
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0501
|2 StatID
|b DOAJ Seal
|d 2024-04-10T15:36:12Z
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0500
|2 StatID
|b DOAJ
|d 2024-04-10T15:36:12Z
915 _ _ |a WoS
|0 StatID:(DE-HGF)0113
|2 StatID
|b Science Citation Index Expanded
|d 2024-12-10
915 _ _ |a Fees
|0 StatID:(DE-HGF)0700
|2 StatID
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
|d 2024-12-10
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a Peer Review
|0 StatID:(DE-HGF)0030
|2 StatID
|b ASC
|d 2024-12-10
915 _ _ |a Article Processing Charges
|0 StatID:(DE-HGF)0561
|2 StatID
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1150
|2 StatID
|b Current Contents - Physical, Chemical and Earth Sciences
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
|d 2024-12-10
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Clarivate Analytics Master Journal List
|d 2024-12-10
920 1 _ |0 I:(DE-H253)MPSD-20120731
|k MPSD
|l Forschungsgruppe für strukturelle Dynamik
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-H253)MPSD-20120731
980 1 _ |a FullTexts

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21