Related Articles(19) F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-?-Lactamase.
Angew Chem Int Ed Engl. 2017 Mar 02;:
Authors: Abboud MI, Hinchliffe P, Brem J, Macsics R, Pfeffer I, Makena A, Umland KD, Rydzik AM, Li GB, Spencer J, Claridge TD, Schofield CJ
Abstract
Resistance to ?-lactam antibiotics mediated by metallo-?-lactamases (MBLs) is a growing problem. We describe the use of protein-observe (19) F-NMR (PrOF NMR) to study the dynamics of the São Paulo MBL (SPM-1) from ?-lactam-resistant Pseudomonas aeruginosa. Cysteinyl variants on the ?3 and L3 regions, which flank the di-Zn(II) active site, were selectively (19) F-labeled using 3-bromo-1,1,1-trifluoroacetone. The PrOF NMR results reveal roles for the mobile ?3 and L3 regions in the binding of both inhibitors and hydrolyzed ?-lactam products to SPM-1. These results have implications for the mechanisms and inhibition of MBLs by ?-lactams and non-?-lactams and illustrate the utility of PrOF NMR for efficiently analyzing metal chelation, identifying new binding modes, and studying protein binding from a mixture of equilibrating isomers.
PMID: 28252254 [PubMed - as supplied by publisher]
[NMR paper] A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Related Articles A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Eur J Med Chem. 2014 Jun 11;83C:92-101
Authors: Sim?i? M, Pureber K, Kristan K, Urleb U, Kocjan D, Grdadolnik SG
Abstract
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide,...
nmrlearner
Journal club
0
06-22-2014 12:24 PM
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
Publication date: Available online 11 June 2014
Source:European Journal of Medicinal Chemistry</br>
Author(s): Mihael Sim?i? , Kaja Pureber , Katja Kristan , Uroš Urleb , Darko Kocjan , Simona Goli? Grdadolnik</br>
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide, an 2-oxoindolinylidene derivative with novel structure scaffold, was evaluated for inhibition potency...
nmrlearner
Journal club
0
06-12-2014 10:52 PM
[NMR paper] Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Related Articles Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Jan 23;
Authors: Ma J, McLeod S, Maccormack K, Sriram S, Gao N, Breeze AL, Hu J
Abstract
Disconnections between in vitro responses and those observed in whole cells confound many attempts to design drugs in areas of serious medical need. A method based on 1D (1) H...
nmrlearner
Journal club
0
01-25-2014 02:07 PM
[NMR paper] The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
Angew Chem Int Ed Engl. 2011 Aug 29;50(36):8432-5
Authors: Higman VA, Varga K, Aslimovska L, Judge PJ, Sperling LJ, Rienstra CM, Watts A
PMID: 21770003
nmrlearner
Journal club
0
03-01-2013 09:57 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...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by m
Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
J Biol Chem. 1995 Sep 1;270(35):20643-52
Authors: Moser MJ, Lee SY, Klevit RE, Davis TN
As a first step toward identifying the important structural elements of...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...
(19) F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-?-Lactamase.
Linear Mode
