Abstract
Peptidoglycan is an essential component of cell wall in Gram-positive bacteria with unknown architecture. In this review, we summarize solid-state NMR approaches to address some of the unknowns in the Gram-positive bacteria peptidoglycan architecture: 1) peptidoglycan backbone conformation, 2) PG-lattice structure, 3) variations in the peptidoglycan architecture and composition, 4) the effects of peptidoglycan bridge-length on the peptidoglycan architecture in Fem mutants, 5) the orientation of glycan strands with respect to the membrane, and 6) the relationship between the peptidoglycan structure and the glycopeptide antibiotic mode of action. Solid-state NMR analyses of Staphylococcus aureus cell wall show that peptidoglycan chains are surprisingly ordered and densely packed. The peptidoglycan disaccharide backbone adopts 4-fold screw helical symmetry with the disaccharide unit periodicity of 40Å. Peptidoglycan lattice in the S. aureus cell wall is formed by cross-linked PG stems that have parallel orientations. The structural characterization of Fem-mutants of S. aureus with varying lengths of bridge structures suggests that the PG-bridge length is an important determining factor for the PG architecture.
[NMR paper] ?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
Proc Natl Acad Sci U S A. 2014 Dec 30;
Authors: Vasa S, Lin L, Shi C, Habenstein B, Riedel D, Kühn J, Thanbichler M, Lange A
Abstract
Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central...
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01-01-2015 11:00 PM
[NMR paper] The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
Related Articles The Na(+) transport in Gram-positive bacteria defect in the Mrp antiporter complex measured with (23)Na-NMR.
Anal Biochem. 2013 Oct 15;
Authors: Górecki K, Hägerhäll C, Drakenberg T
Abstract
(23)Na-NMR has previously been used to monitor Na(+) translocation across membranes in Gram-negative bacteria and in various other organelles and liposomes using a membrane-impermeable shift reagent to resolve the signals...
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10-23-2013 03:49 AM
[NMR paper] Investigation of proteins in living bacteria with in-cell NMR experiments.
Investigation of proteins in living bacteria with in-cell NMR experiments.
Related Articles Investigation of proteins in living bacteria with in-cell NMR experiments.
Top Curr Chem. 2008;273:203-14
Authors: Dötsch V
Abstract
In recent years NMR methods have been developed that enable the observation of proteins insideliving bacterial cells. Because of the sensitivity of the chemical shift to environmental changesthese in-cell NMR experiments can be used to study protein conformation, molecular interaction ordynamics in a*protein's natural...
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04-24-2013 09:48 PM
[NMR paper] Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
Biochemistry. 2012 Oct 16;51(41):8143-53
Authors: Zhou X, Cegelski L
Abstract
The bacterial cell wall is essential to cell survival and is a major target of antibiotics. The main component of the...
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04-02-2013 07:23 PM
Nutrient-Dependent StructuralChanges in S.aureus Peptidoglycan Revealed by Solid-State NMR Spectroscopy
Nutrient-Dependent StructuralChanges in S.aureus Peptidoglycan Revealed by Solid-State NMR Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi3012115/aop/images/medium/bi-2012-012115_0011.gif
Biochemistry
DOI: 10.1021/bi3012115
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/KQGbaoLxmUQ
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Bacteria disarmer activates fiber formation in Parkinson's protein - HealthCanal.com
Bacteria disarmer activates fiber formation in Parkinson's protein - HealthCanal.com
<img alt="" height="1" width="1" />
Bacteria disarmer activates fiber formation in Parkinson's protein
HealthCanal.com
Most of the study was carried out by post-doctoral fellows Istvan Horvath, Christoph F. Weise, and Emma Andersson. With the assistance of the KBC platform for nuclear magnetic resonance, NMR, the scientists have been able to study proteins at the ...
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02-16-2012 08:25 PM
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Feb;49(2):65-9
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the...
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01-22-2011 01:52 PM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Jan 3;
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
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