Alternate pathways for folding in the flavodoxin fold family revealed by a nucleation-growth model.
A recent study of experimental results for flavodoxin-like folds suggests that proteins from this family may exhibit a similar, signature pattern of folding intermediates. We study the folding landscapes of three proteins from the flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model that accurately describes both experimental and simulation results for the transition state structure, and the structure of on-pathway and misfolded intermediates for CheY. Although the landscape features of these proteins agree in basic ways with the results of the study, the simulations exhibit a range of folding behaviours consistent with two alternate folding routes corresponding to nucleation and growth from either side of the central beta-strand.
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 6001 Forest Park Blvd., Room ND10.124, Dallas, TX 75235-9050, USA. enelson@spirit.sdsc.edu
Erik D
ED
Nelson
Nick V
NV
Grishin
D001059:Apoproteins / Q000737:chemistry / Q000378:metabolism; D005418:Flavodoxin / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D001059:Apoproteins; D005418:Flavodoxin; D008565:Membrane Proteins