Phage tailspike proteins with beta-solenoid fold as thermostable carbohydrate binding materials.
We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable beta-solenoid folds and similarly high kinetic stability in spite of different amino acid sequences. As tailspikes bind polysaccharides to recognize the bacterial host cell, their stability is required for maintenance of bacteriophage infectivity under harsh extracellular conditions. They resist denaturation by SDS at ambient temperature and their unfolding is slow even in 6 M guanidinium hydrochloride (GdmHCl). This makes them interesting candidates for very stable carbohydrate binding protein materials.
Barbirz
Stefanie
S
Physikalische Biochemie, Universität Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Golm, Germany.
Becker
Marion
M
Freiberg
Alexander
A
Seckler
Robert
R
D002241:Carbohydrates / Q000737:chemistry*; D006026:Glycoside Hydrolases; D019791:Guanidine / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D011489:Protein Denaturation; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013696:Temperature; D017376:Viral Tail Proteins / Q000737:chemistry*
D002241:Carbohydrates; D017376:Viral Tail Proteins; D012967:Sodium Dodecyl Sulfate; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage; D019791:Guanidine