Structure of BT-3984, a member of the SusD/RagB family of nutrient-binding molecules

Abstract

The crystal structure of the Bacteroides thetaiotaomicron protein BT-3984 was determined to a resolution of 1.7 Å and was the first structure to be determined from the extensive SusD family of polysaccharide-binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT-3984 revealed an N-terminal region containing several tetratricopeptide repeats (TPRs), while the signature C-terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT-3984 suggests the presence of binding interfaces for other proteins from the polysaccharide-utilization complex.