A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution

Qingping Xu, 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, David Marciano, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Christina Puckett, Ron Reyes, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Henry Van Den Bedem, Dana Weekes, Tiffany Wooten, Andrew Yeh, Jiadong Zhou, Keith O. Hodgson, John Wooley, Marc Andre Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of the minor fimbriae in Porphyromonas gingivalis. The crystal structure of BT1062 revealed a conserved fold that is widely adopted by fimbrial components.

Original languageEnglish (US)
Pages (from-to)1281-1286
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number10
DOIs
StatePublished - Oct 1 2010

Keywords

  • BT1062
  • DUF1812
  • Mfa2
  • PF08842
  • PG0179
  • PGN0288
  • fimbriae
  • pili

ASJC Scopus subject areas

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

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    Xu, Q., 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). A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(10), 1281-1286. https://doi.org/10.1107/S1744309110006548