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

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 66; no. 10; p. 1281
• Main Authors: Xu, Qingping, Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L, Bakolitsa, Constantina, Cai, Xiaohui, Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Chiu, Michelle, Clayton, Thomas, Das, Debanu, Deller, Marc C, Duan, Lian, Ellrott, Kyle, Farr, Carol L, Feuerhelm, Julie, Grant, Joanna C, Grzechnik, Anna, Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K, Klock, Heath E, Knuth, Mark W, Kozbial, Piotr, Krishna, S Sri, Kumar, Abhinav, Marciano, David, McMullan, Daniel, Miller, Mitchell D, Morse, Andrew T, Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Puckett, Christina, Reyes, Ron, Sefcovic, Natasha, Tien, Henry J, Trame, Christine B, Van Den Bedem, Henry, Weekes, Dana, Wooten, Tiffany, Yeh, Andrew, Zhou, Jiadong, Hodgson, Keith O, Wooley, John, Elsliger, Marc-Andre, Deacon, Ashley M, Godzik, Adam, Lesley, Scott A, Wilson, Ian A
• Format: Journal Article
• Language: English
• Published: Chester Wiley Subscription Services, Inc 01-10-2010
• Subjects: Bacteriology; Crystal structure; Hemoglobin
• ISSN: 2053-230X
• DOI: 10.1107/S1744309110006548

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.