Characterization of folding pathways of the type-1 and type-2 periplasmic binding proteins MglB and ArgT.
The family of periplasmic binding proteins (PBPs) is believed to have arisen from a common ancestor and to have differentiated into two types. At first approximation, both types of PBPs have the same fold pattern, reflecting their common origin. However, the connection between the main chains of a type 2 PBP is more complicated than a type 1 PBP's. We have been interested in the possibility that such structural changes affect the folding of PBPs. In this study, we have characterized the folding pathways of MglB (a type 1 PBP) and ArgT (a type 2 PBP) by using urea gradient gel electrophoresis, fast protein size-exclusion liquid chromatography and hydrophobic dye ANS binding assay. We found a distinct difference in folding between these two proteins. The folding of MglB followed a simple two-state transition model, whereas the folding of ArgT was more complicated.
Kashiwagi
Kenji
K
School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526, Japan.
Shiba
Kiyotaka
K
Fukami-Kobayashi
Kaoru
K
Noda
Tetsuo
T
Nishikawa
Ken
K
Noguchi
Hiroshi
H
D001693:Biological Transport, Active; D033902:Periplasmic Binding Proteins / Q000032:analysis / Q000737:chemistry* / Q000145:classification; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology
D033902:Periplasmic Binding Proteins