Interaction between a type-II dockerin domain and a type-II cohesin domain from Clostridium thermocellum cellulosome.
The interaction between the type-II dockerin domain of the scaffoldin protein CipA and the type-II cohesin domain of the outer layer protein SdbA is the fundamental mechanism for anchoring the cellulosome to the cell surface of Clostridium thermocellum. We constructed and purified a dockerin polypeptide and a cohesin polypeptide, and determined affinity constants of the interaction between them by the surface plasmon resonance method. The dissociation constant (K(D)) value was 1.8 x 10(-9) M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.
Jindou
Sadanari
S
Faculty of Bioresources, Mie University, Tsu, Japan.
Kajino
Tsutomu
T
Inagaki
Minoru
M
Karita
Shuichi
S
Beguin
Pierre
P
Kimura
Tetsuya
T
Sakka
Kazuo
K
Ohmiya
Kunio
K
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D018797:Cell Cycle Proteins; D044603:Cellulosomes / Q000737:chemistry* / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone; D003013:Clostridium / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D020349:Surface Plasmon Resonance; D000097722:Cohesins
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D005656:Fungal Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins; D000097722:Cohesins; C080369:CipA protein, Clostridium; C093327:OlpB protein, Clostridium thermocellum; C105449:SdbA protein, bacteria