An off-pathway folding intermediate of an acyl carrier protein domain coexists with the folded and unfolded states under native conditions.
A protein can exist in multiple states under native conditions and those states with low populations are often critical to biological function and self-assembly. To investigate the role of the minor states of an acyl carrier protein, NMR techniques were applied to determine the number of minor states and characterize their structures and kinetics. The acyl carrier protein from Micromonospora echinospora was found to exist in one major folded state (95.2%), one unfolded state (4.1%), and one intermediate state (0.7%) under native conditions. The three states are in dynamic equilibrium and the intermediate state very likely adopts a native-like structure and is an off-pathway folding product. The intermediate state may mediate the formation of oligomers in vitro and play an important role in the recognition of partner enzymes in vivo.
Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543 (Singapore).
Jackwee
J
Lim
Tianshu
T
Xiao
Jingsong
J
Fan
Daiwen
D
Yang
D000213:Acyl Carrier Protein / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D007700:Kinetics; D008847:Micromonospora / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins
acyl carrier protein; folding intermediates; protein dynamics; protein folding; protein structure