Structure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: The first structural representative of a new protein family that may play a role in carbohydrate metabolism

Andrew P. Yeh, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Constantina Bakolitsa, Xiaohui Cai, Dennis Carlton, Connie Chen, Hsiu Ju Chiu, Michelle Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Kyle Ellrott, Carol L. Farr, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Gye Won HanLukasz Jaroszewski, Kevin 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, Tiffany Wooten, Qingping Xu, Keith O. Hodgson, John Wooley, Marc André Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

BT2081 from Bacteroides thetaiotaomicron (GenBank accession code NP-810994.1) is a member of a novel protein family consisting of over 160 members, most of which are found in the different classes of Bacteroidetes. Genome-context analysis lends support to the involvement of this family in carbohydrate metabolism, which plays a key role in B. thetaiotaomicron as a predominant bacterial symbiont in the human distal gut microbiome. The crystal structure of BT2081 at 2.05 Å resolution represents the first structure from this new protein family. BT2081 consists of an N-terminal domain, which adopts a β-sandwich immunoglobulin-like fold, and a larger C-terminal domain with a β-sandwich jelly-roll fold. Structural analyses reveal that both domains are similar to those found in various carbohydrate-active enzymes. The C-terminal Β-jelly-roll domain contains a potential carbohydrate-binding site that is highly conserved among BT2081 homologs and is situated in the same location as the carbohydrate-binding sites that are found in structurally similar glycoside hydrolases (GHs). However, in BT2081 this site is partially occluded by surrounding loops, which results in a deep solvent-accessible pocket rather than a shallower solvent-exposed cleft.

Original languageEnglish (US)
Pages (from-to)1287-1296
Number of pages10
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number10
DOIs
StatePublished - Oct 1 2010

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Keywords

  • gut microbiome
  • immunoglobulin-like fold
  • jelly-roll fold
  • structural genomics
  • sugars

ASJC Scopus subject areas

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

Cite this

Yeh, A. P., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Cai, X., Carlton, D., Chen, C., Chiu, H. J., Chiu, M., Clayton, T., Das, D., Deller, M. C., Duan, L., Ellrott, K., Farr, C. L., Feuerhelm, J., Grant, J. C., Grzechnik, A., ... Wilson, I. A. (2010). Structure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: The first structural representative of a new protein family that may play a role in carbohydrate metabolism. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(10), 1287-1296. https://doi.org/10.1107/S1744309110028228