- Main
Structure of BT_3984, a member of the SusD/RagB family of nutrient‐binding molecules
- Bakolitsa, Constantina;
- Xu, Qingping;
- Rife, Christopher L;
- Abdubek, Polat;
- Astakhova, Tamara;
- Axelrod, Herbert L;
- Carlton, Dennis;
- Chen, Connie;
- Chiu, Hsiu-Ju;
- Clayton, Thomas;
- Das, Debanu;
- Deller, Marc C;
- Duan, Lian;
- Ellrott, Kyle;
- Farr, Carol L;
- Feuerhelm, Julie;
- Grant, Joanna C;
- Grzechnik, Anna;
- Han, Gye Won;
- Jaroszewski, Lukasz;
- Jin, Kevin K;
- Klock, Heath E;
- Knuth, Mark W;
- Kozbial, Piotr;
- Krishna, S Sri;
- Kumar, Abhinav;
- Lam, Winnie W;
- Marciano, David;
- McMullan, Daniel;
- Miller, Mitchell D;
- Morse, Andrew T;
- Nigoghossian, Edward;
- Nopakun, Amanda;
- Okach, Linda;
- Puckett, Christina;
- Reyes, Ron;
- Tien, Henry J;
- Trame, Christine B;
- van den Bedem, Henry;
- Weekes, Dana;
- Hodgson, Keith O;
- Wooley, John;
- Elsliger, Marc-André;
- Deacon, Ashley M;
- Godzik, Adam;
- Lesley, Scott A;
- Wilson, Ian A
- et al.
Published Web Location
https://doi.org/10.1107/s1744309110032999Abstract
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.
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