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 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
October, 2010
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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.

Type
Journal article
Publication
Acta crystallographica. Section F, Structural biology and crystallization communications