title: Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold.
abstract: The topology of a native protein influences the rate with which it is formed, but does topology affect the appearance of folding intermediates and their specific role in kinetic folding as well? This question is addressed by comparing the folding data recently obtained on apoflavodoxin from Azotobacter vinelandii with those available on all three other alpha-beta parallel proteins the kinetic folding mechanism of which has been studied, i.e. Anabaena apoflavodoxin, Fusarium solani pisi cutinase and CheY. Two kinetic folding intermediates, one on-pathway and the other off-pathway, seem to be present during the folding of proteins with an alpha-beta parallel, also called flavodoxin-like, topology. The on-pathway intermediate lies on a direct route from the unfolded to the native state of the protein involved. The off-pathway intermediate needs to unfold to allow the production of native protein. Available simulation data of the folding of CheY show the involvement of two intermediates with characteristics that resemble those of the two intermediates experimentally observed. Apparently, protein topology governs the appearance and kinetic roles of protein folding intermediates during the folding of proteins that have a flavodoxin-like fold.
authors.affiliation: Department of Agrotechnology and Food Sciences, Laboratory of Biochemistry, Wageningen University, The Netherlands.
authors.forename: Yves J M
authors.initials: YJ
authors.lastname: Bollen
authors.forename: Carlo P M
authors.initials: CP
authors.lastname: van Mierlo
mesh_terms: D017033:Anabaena / Q000737:chemistry; D001059:Apoproteins / Q000737:chemistry; D016948:Azotobacter vinelandii / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry; D005418:Flavodoxin / Q000737:chemistry*; D005670:Fusarium / Q000201:enzymology; D008565:Membrane Proteins / Q000737:chemistry; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D001059:Apoproteins; D001426:Bacterial Proteins; D005418:Flavodoxin; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C026932:apoflavodoxin; D002265:Carboxylic Ester Hydrolases; C019952:cutinase