Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.

ABSTRACT: Streptococcus gordonii is a member of the viridans streptococci and is an early colonizer of the tooth surface. Adherence to the tooth surface is enabled by proteins present on the S. gordonii cell surface, among which SspB belongs to one of the most well studied cell-wall-anchored adhesin families: the antigen I/II (AgI/II) family. The C-terminal region of SspB consists of three tandemly connected individual domains that display the DEv-IgG fold. These C-terminal domains contain a conserved Ca²⁺-binding site and isopeptide bonds, and they adhere to glycoprotein 340 (Gp340; also known as salivary agglutinin, SAG). Here, the structural and functional characterization of the C₁₂₃^SspB domain at 2.7 Å resolution is reported. Although the individual C-terminal d

SUBMITTER: Schormann N 

PROVIDER: S-EPMC8411976 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature