High-affinity interaction between the S-layer protein SbsC and the secondary cell wall polymer of Geobacillus stearothermophilus ATCC 12980 determined by surface plasmon resonance technology.
Surface plasmon resonance studies using C-terminal truncation forms of the S-layer protein SbsC (recombinant SbsC consisting of amino acids 31 to 270 [rSbsC(31-270)] and rSbsC(31-443)) and the secondary cell wall polymer (SCWP) isolated from Geobacillus stearothermophilus ATCC 12980 confirmed the exclusive responsibility of the N-terminal region comprising amino acids 31 to 270 for SCWP binding. Quantitative analyses indicated binding behavior demonstrating low, medium, and high affinities.
Ferner-Ortner
Judith
J
Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences, Gregor Mendel-Strasse 33, A-1180 Vienna, Austria.
Mader
Christoph
C
Ilk
Nicola
N
Sleytr
Uwe B
UB
Egelseer
Eva M
EM
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D020349:Surface Plasmon Resonance / Q000379:methods*
D001426:Bacterial Proteins; D010446:Peptide Fragments