title: 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.
authors.affiliation: Department of Chemistry and Biochemistry, Baylor University , Waco, Texas 76706, United States.
authors.forename: Sung Joon
authors.initials: SJ
authors.lastname: Kim
authors.forename: Manmilan
authors.initials: M
authors.lastname: Singh
authors.forename: Maria
authors.initials: M
authors.lastname: Preobrazhenskaya
authors.forename: Jacob
authors.initials: J
authors.lastname: Schaefer
mesh_terms: D002455:Cell Division; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010457:Peptidoglycan / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000166:cytology
chemical_list: D010457:Peptidoglycan