Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.
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DOI:
10.1016/j.bbamem.2014.05.031
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发表时间:
2015-01
期刊:
影响因子:
--
通讯作者:
Singh M
中科院分区:
文献类型:
--
作者:
Kim SJ;Chang J;Singh M
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 respect to the membrane, and 6) the relationship between the peptidoglycan structure and the glycopeptide antibiotic mode of action. Solid-state NMR analyses of S. 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 40 Å. Peptidoglycan lattice in 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.
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