Related ArticlesNMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.
Eur Biophys J. 2020 Mar 09;:
Authors: Golubev A, Fatkhullin B, Gabdulkhakov A, Bikmullin A, Nurullina L, Garaeva N, Islamov D, Klochkova E, Klochkov V, Aganov A, Khusainov I, Validov S, Yusupova G, Yusupov M, Usachev K
Abstract
Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48*Å resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.
PMID: 32152681 [PubMed - as supplied by publisher]
[NMR paper] Solid-state NMR characterization of amphomycin effects on peptidoglycan and wall teichoic acid biosyntheses in Staphylococcus aureus.
Solid-state NMR characterization of amphomycin effects on peptidoglycan and wall teichoic acid biosyntheses in Staphylococcus aureus.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.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 Solid-state NMR characterization of amphomycin effects on peptidoglycan and wall teichoic acid biosyntheses in Staphylococcus aureus.
Sci Rep. 2016 08 19;6:31757
Authors:...
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[NMR paper] NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF).
NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF).
NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF).
Biomol NMR Assign. 2017 Oct 04;:
Authors: Usachev KS, Ayupov RK, Validov SZ, Khusainov IS, Yusupov MM
Abstract
Staphylococcus aureus: hibernation-promoting factor (SaHPF) is a 22.2*kDa stationary-phase protein that binds to the ribosome and turns it to the inactive form favoring survival under stress. Sequence analysis has...
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[NMR paper] NMR Structure-Based Optimization of Staphylococcus aureus Sortase A Pyridazinone Inhibitors.
NMR Structure-Based Optimization of Staphylococcus aureus Sortase A Pyridazinone Inhibitors.
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Chem Biol Drug Des. 2017 Feb 03;:
Authors: Chan AH, Yi SW, Weiner EM, Amer BR, Sue CK, Wereszczynski J, Dillen CA, Senese S, Torres JZ, Andrew McCammon J, Miller LS, Jung ME, Clubb RT
Abstract
Staphylococcus aureus is a leading cause of hospital-acquired infections in the United States and is a major health concern as...
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[NMR paper] Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
Biochemistry. 2013 May 28;52(21):3651-9
Authors: Kim SJ, Singh M, Preobrazhenskaya M, Schaefer J
Abstract
Staphylococcus aureus grown in the presence of an alanine-racemase inhibitor was labeled with d-alanine...
[NMR paper] Identification of residues involved in the interaction of Staphylococcus aureus fibro
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
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Biochemistry. 2000 Mar 21;39(11):2887-93
Authors: Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR
Many...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...