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.
Original language | English (US) |
---|---|
Pages (from-to) | 1274-1280 |
Number of pages | 7 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2010 |
Externally published | Yes |
Keywords
- gut microbiome
- metagenomics
- starch-utilization system
- structural genomics
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics