{Reference Type}: Journal Article
{Title}: Crystal structure of the long Rib domain of the LPXTG-anchored surface protein from Limosilactobacillus reuteri.
{Author}: Xue Y;Wu Z;Kang X;
{Journal}: Acta Crystallogr F Struct Biol Commun
{Volume}: 80
{Issue}: 0
{Year}: 2024 May 1
{Factor}: 1.072
{DOI}: 10.1107/S2053230X24003868
{Abstract}: The Rib domain, which is often found as tandem-repeat structural modules in surface proteins of Gram-positive bacteria, plays important roles in mediating interactions of bacteria with their environments and hosts. A comprehensive structural analysis of various Rib domains is essential to fully understand their impact on the structure and functionality of these bacterial adhesins. To date, structural information has been limited for this expansive group of domains. In this study, the high-resolution crystal structure of the second member of the long Rib domain, a unique subclass within the Rib-domain family, derived from Limosilactobacillus reuteri is presented. The data not only demonstrate a highly conserved structure within the long Rib domain, but also highlight an evolutionary convergence in structural architecture with other modular domains found in cell-adhesion molecules.