title: Cross-link formation and peptidoglycan lattice assembly in the FemA mutant of Staphylococcus aureus.
abstract: Staphylococcus aureus FemA mutant grown in the presence of an alanine-racemase inhibitor was labeled with d-[1-(13)C]alanine, l-[3-(13)C]alanine, [2-(13)C]glycine, and l-[5-(19)F]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 (13)C-labeled alanines and (19)F-labeled lysine incorporated in the peptidoglycan. The alanyl (13)C labels were preselected for REDOR measurement by their proximity to the glycine label using (13)C-(13)C spin diffusion. The observed (13)C-(13)C and (13)C-(19)F distances are consistent with a tightly packed, hybrid architecture containing both parallel and perpendicular stems in a repeating structural motif within the peptidoglycan.
authors: Department of Chemistry and Biochemistry, Baylor University , Waco, Texas 76706, United States.
authors: Sung Joon
authors: SJ
authors: Kim
authors: Manmilan
authors: M
authors: Singh
authors: Shasad
authors: S
authors: Sharif
authors: Jacob
authors: J
authors: Schaefer
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D002853:Chromatography, Liquid; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D010457:Peptidoglycan / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D010457:Peptidoglycan