Structural Characteristics of Pneumolysin and Its Domains in a Biomimetic Solution.

ABSTRACT: Pneumolysin (PLY) and its truncated fragments, domains 1-3 (D_1-3), and domain 4 (D₄), were purified as recombinant proteins after being cloned and over-expressed in Escherichia coli. The three-dimensional structures of these proteins were quantitatively investigated in a biomimetic condition, phosphate buffered saline (PBS) by synchrotron X-ray scattering. X-ray scattering analysis revealed important structural features including structural parameters. PLY was present as a monomeric form in PBS. The monomeric form resembled its crystallographic structure with a discrepancy of only 6.3%, confirming that PLY forms a stable structure and, thus, retains its structure in the crystalline state and even in PBS solution. D₄ was also present as a monomeric fo

SUBMITTER: Lee J 

PROVIDER: S-EPMC6644606 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature