Structural comparison of acyl carrier protein in acylated and sulfhydryl forms by two-dimensional 1H NMR spectroscopy.
Sequence-specific assignments of 1H NMR resonances are obtained for the backbone protons of Escherichia coli acyl carrier protein, acylated with an eight-carbon chain covalently attached to the prosthetic group thiol (octanoyl-ACP). Comparison of 1H-1H sequential connectivities in the NOESY spectra of octanoyl-ACP and the unacylated protein (ACPSH) indicates that secondary structure is largely conserved on acylation. Changes in resonance positions observed for certain groups of residues are interpreted in terms of a model that describes the spatial reorientation of secondary structural elements in the protein resulting from introduction of the acyl chain.
Jones
P J
PJ
Department of Chemistry, Yale University, New Haven, Connecticut 06511.
Holak
T A
TA
Prestegard
J H
JH
D000213:Acyl Carrier Protein / Q000378:metabolism*; D000215:Acylation; D004926:Escherichia coli / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D013438:Sulfhydryl Compounds
D000213:Acyl Carrier Protein; D013438:Sulfhydryl Compounds