[NMR paper] Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC beta-Lactamase
Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC beta-Lactamase
?-Lactamase-mediated resistance to ceftazidime-avibactam (CZA) is a serious limitation in the treatment of Gram-negative bacteria harboring Klebsiella pneumoniae carbapenemase (KPC). Herein, the basis of susceptibility to carbapenems and resistance to ceftazidime (CAZ) and CZA of the D179Y variant of KPC-2 and -3 was explored. First, we determined that resistance to CZA in a laboratory strain of Escherichia coli DH10B was not due to increased expression levels of the variant enzymes, as...
[NMR paper] Biphasic activation of beta-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR
Biphasic activation of beta-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR
?-arrestins (?arrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). ?arrs typically interact with phosphorylated C-terminal tail (C tail) and transmembrane core (TM core) of GPCRs. However, the effects of the C tail- and TM core-mediated interactions on the conformational activation of ?arrs have remained elusive. Here, we show the conformational changes for ?arr activation upon the C tail- and TM core-mediated interactions with a prototypical GPCR by nuclear......
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12-10-2021 07:19 PM
Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam
Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam
Abstract
Backbone chemical shift assignments for the Toho-1 β-lactamase (263 amino acids, 28.9Â*kDa) are reported based on triple resonance solution-state NMR experiments performed on a uniformly 2H,13C,15N-labeled sample. These assignments allow for subsequent site-specific characterization at the chemical, structural, and dynamical levels. At the chemical level, titration with the non-β-lactam β-lactamase inhibitor avibactam is found to...
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07-04-2021 10:41 AM
[NMR paper] Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
Biophys J. 2021 Jan 29;:
Authors: Xu X, Gagné D, Aramini JM, Gardner KH
Abstract
Proteins often interconvert between different conformations in ways critical to their function. While manipulating...
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02-03-2021 01:55 AM
[NMR paper] Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.
Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.
Proc Natl...
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03-27-2018 09:54 PM
[NMR paper] NMR backbone resonance assignment of New Delhi metallo-beta-lactamase.
NMR backbone resonance assignment of New Delhi metallo-beta-lactamase.
Related Articles NMR backbone resonance assignment of New Delhi metallo-beta-lactamase.
Biomol NMR Assign. 2017 Aug 14;:
Authors: Yao C, Wu Q, Xu G, Li C
Abstract
The emerging of the New Delhi metallo-beta-lactamase (NDM-1) has become one of the greatest threats to the clinical treatment. Although the structure of NDM-1 has been determined by X-ray crystallography, the molecular mechanism and process of catalysis reaction remain elusive. NMR spectroscopy plays...
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08-17-2017 01:01 PM
[NMR paper] Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.
Nat Commun. 2015;6:8202
Authors: Yang F, Yu X, Liu C, Qu CX, Gong Z, Liu HD, Li FH, Wang HM, He DF, Yi F, Song C, Tian CL, Xiao KH, Wang JY, Sun JP
Abstract
Specific arrestin conformations are coupled to distinct downstream effectors, which underlie the functions of many...
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09-09-2015 11:49 AM
[NMR paper] pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.
pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles pH-triggered, activated-state conformations of the influenza hemagglutinin fusion...
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02-07-2013 10:31 PM
[NMR paper] NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its
NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Related Articles NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Biochemistry. 1999 Nov 2;38(44):14507-14
Authors: Scrofani SD, Chung J, Huntley JJ, Benkovic SJ, Wright PE, Dyson HJ
Understanding the structure and dynamics of the enzymes that mediate antibiotic resistance of...
Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC beta-Lactamase
Linear Mode
