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

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.

SUBMITTER: Kim SJ

PROVIDER: S-EPMC3796188 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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

Kim Sung Joon SJ Singh Manmilan M Preobrazhenskaya Maria M Schaefer Jacob J

Biochemistry 20130514 21

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) ...[more]

PMID: 23617832

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