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

Constantina Bakolitsa, Qingping Xu, Christopher L. Rife, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Dennis Carlton, Connie Chen, Hsiu Ju Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Kyle Ellrott, Carol L. Farr, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Gye Won Han, Lukasz JaroszewskiKevin K. Jin, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, S. Sri Krishna, Abhinav Kumar, Winnie W. Lam, David Marciano, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Christina Puckett, Ron Reyes, Henry J. Tien, Christine B. Trame, Henry Van Den Bedem, Dana Weekes, Keith O. Hodgson, John Wooley, Marc André Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

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 languageEnglish (US)
Pages (from-to)1274-1280
Number of pages7
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number10
DOIs
StatePublished - Oct 2010
Externally publishedYes

Keywords

  • gut microbiome
  • metagenomics
  • starch-utilization system
  • structural genomics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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