Cross-Link Formation and Peptidoglycan Lattice Assembly in the FemA Mutant of Staphylococcus aureus

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• 作者：Sung Joon Kim ; Manmilan Singh ; Shasad Sharif ; Jacob Schaefer
• 刊名：Biochemistry
• 出版年：2014
• 出版时间：March 11, 2014
• 年：2014
• 卷：53
• 期：9
• 页码：1420-1427
• 全文大小：532K
• 年卷期：v.53,no.9(March 11, 2014)
• ISSN：1520-4995

文摘

Staphylococcus aureus FemA mutant grown in the presence of an alanine-racemase inhibitor was labeled with d-[1-¹³C]alanine, l-[3-¹³C]alanine, [2-¹³C]glycine, and l-[5-¹⁹F]lysine to characterize some details of the peptidoglycan tertiary structure. Rotational-echo double-resonance (REDOR) NMR of isolated cell walls was used to measure internuclear distances between ¹³C-labeled alanines and ¹⁹F-labeled lysine incorporated in the peptidoglycan. The alanyl ¹³C labels were preselected for REDOR measurement by their proximity to the glycine label using ¹³C鈥?sup>13C spin diffusion. The observed ¹³C鈥?sup>13C and ¹³C鈥?sup>19F distances are consistent with a tightly packed, hybrid architecture containing both parallel and perpendicular stems in a repeating structural motif within the peptidoglycan.