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

نویسندگان

  • 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 Han
  • Lukasz 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
چکیده

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.

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عنوان ژورنال:

دوره 66  شماره 

صفحات  -

تاریخ انتشار 2010