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Literature DB >> 23617832

Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.

Sung Joon Kim¹, Manmilan Singh, Maria Preobrazhenskaya, Jacob Schaefer.

Abstract

Staphylococcus aureus grown in the presence of an alanine-racemase inhibitor was labeled with d-[1-(13)C]alanine and l-[(15)N]alanine to characterize some details of the peptidoglycan tertiary structure. Rotational-echo double-resonance NMR of intact whole cells was used to measure internuclear distances between (13)C and (15)N of labeled amino acids incorporated in the peptidoglycan, and from those labels to (19)F of a glycopeptide drug specifically bound to the peptidoglycan. The observed (13)C-(15)N average distance of 4.1-4.4 Å between d- and l-alanines in nearest-neighbor peptide stems is consistent with a local, tightly packed, parallel-stem architecture for a repeating structural motif within the peptidoglycan of S. aureus.

Entities: Chemical Disease Gene Species

Mesh：

Substances：
Peptidoglycan

Year: 2013 PMID： 23617832 PMCID： PMC3796188 DOI： 10.1021/bi4005039

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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