Biophysical characterization and solution structure of the cannulae-forming protein CanA from the hyperthermophilic archaeon Pyrodictium abyssi.

ABSTRACT: CanA from Pyrodictium abyssi, the main constituent of the extracellular protein network of this archaeon, forms a hollow-fiber network in the presence of divalent ions. The polymerization of CanA induced by divalent ions is characterized by (at least) two processes with rate constants of 0.19 and 0.03 ms^-1 at 298 K with a critical monomer concentration of 2.48 µM. A non-polymerizing mutant, K₁-CanA, was created, and the NMR solution structure could be determined by multidimensional NMR spectroscopy. It mainly consists of β-pleated sheets and 2 small α-helices, arranged as β₁β₂β₃β₄α₁β₅β₆α₂β₇β₈β₉β₁₀β₁₁β₁₂β₁₃

SUBMITTER: Munte CE 

PROVIDER: S-EPMC12326000 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature