Staphylococcus aureus Peptidoglycan Stem Packing by Rotational-Echo Double Resonance NMR Spectroscopy

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• 作者：Sung Joon Kim ; Manmilan Singh ; Maria Preobrazhenskaya ; Jacob Schaefer
• 刊名：Biochemistry
• 出版年：2013
• 出版时间：May 28, 2013
• 年：2013
• 卷：52
• 期：21
• 页码：3651-3659
• 全文大小：478K
• 年卷期：v.52,no.21(May 28, 2013)
• ISSN：1520-4995

文摘

Staphylococcus aureus grown in the presence of an alanine-racemase inhibitor was labeled with d-[1-¹³C]alanine and l-[¹⁵N]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 ¹³C and ¹⁵N of labeled amino acids incorporated in the peptidoglycan, and from those labels to ¹⁹F of a glycopeptide drug specifically bound to the peptidoglycan. The observed ¹³C鈥?sup>15N average distance of 4.1鈥?.4 脜 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.