Structure of a SusD homologue, BT1043, involved in mucin O-glycan utilization in a prominent human gut symbiont.

ABSTRACT: Mammalian distal gut bacteria have an expanded capacity to utilize glycans. In the absence of dietary sources, some species rely on host-derived mucosal glycans. The ability of Bacteroides thetaiotaomicron, a prominent human gut symbiont, to forage host glycans contributes to both its ability to persist within an individual host and its ability to be transmitted naturally to new hosts at birth. The molecular basis of host glycan recognition by this species is still unknown but likely occurs through an expanded suite of outermembrane glycan-binding proteins that are the primary interface between B. thetaiotaomicron and its environment. Presented here is the atomic structure of the B. thetaiotaomicron protein BT1043, an outer membrane lipoprotein involved in host glycan metabolism. Despite a

SUBMITTER: Koropatkin N 

PROVIDER: S-EPMC2655733 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature