Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1274-80. doi: 10.1107/S1744309110032999. Epub 2010 Sep 22.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacteroides / chemistry*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Structural Homology, Protein

Substances

  • Bacterial Proteins

Associated data

  • PDB/3CGH